新型β-葡萄糖苷酶菌株syzx4筛选、发酵及酶纯化表征和应用
|
摘要
本研究从腐败的玉米秸秆上分离得到一株能够发酵生产耐热耐酸性的β-葡萄糖苷酶的菌株,经过形态学和分子生物学方法的鉴定为Tolypocladium cylindrosporum syzx4。然后利用计算机辅助的方法对此菌株的发酵培养基进行了优化,菌株的筛选过程和酶的发酵过程申请了国家专利。
首先,使用Plackett-Burmans实验设计法对碳源、氮源和无机盐进行产酶显著性的分析,培养基组分对β-葡萄糖苷酶生产影响排序为：TCS>KH2PO4> SM=(NH4)2SO4;然后应用计算机辅助模型拟合的方法对培养基进行进一步的优化,建立的模型包括响应面法和人工智能,人工智能模型表现的非常优异,得到的最佳培养基组成为：TCS 26.274 g/L,SM 7.066 g/L, KH2PO41.991 g/L, (NH4)2SO42.328 g/L,其它成分保持原始值,30℃,初始pH值为5时,发酵8天,此时发酵生产的β-葡萄糖苷酶活力可以达到2.714U/mL。
接下来对Tolypocladium cylindrosporum syzx4发酵生产的β-葡萄糖苷酶进行纯化、性质分析、糖化和同步糖化发酵气爆玉米秸秆的应用研究。酶的纯化过程采用的是硫酸铵沉淀法,DEAE-52纤维素离子交换法和Sephadex G-100凝胶层析法。纯化后相对于纯化前的粗酶液活力提高了9.47倍,回收率为12.27%,得到的酶活力为40.50U/mL。SDS-PAGE结果显示为分子量为58.6 kDa的一条带,表明达到了电泳纯,Native-PAGE的结果表明此β-葡萄糖苷酶表现出良好的生物活性。酶学性质分析以β-葡萄糖苷酶对常用的三种水解底物为对象即纤维二糖,水杨素和p-NPG,研究了酶的水解性质,水杨素为底物时Km为8.8 mmoL/L Vmax为25.6 mmoL/s和Kcat为53.89 s-1；以纤维二糖为底物时得到Km为2.59mmoL/L、Vmax为45.3 mmoL/s和Kcat为95.37s-1；对硝基苯-β-D葡萄糖苷(p-NPG)为底物时得到Km为0.85 mmoL/Lmax为85.23 mmoL/s和Kcat为179.43s-1；以p-NPG为底物时,酶对葡萄糖的抑制常数Ki为3.95 mmoL/L,对葡萄糖醛酸内酯的抑制常数Ki为13.29μmol/L,β-葡萄糖苷水解酶具有较强的耐受葡萄糖和葡萄糖醛酸内酯的的性能,温度和pH值对酶活性的影响分析表明广泛的温度适应性在35到70℃反应时酶活性保留了85%以上；该酶耐酸性很强,在pH值为3.0时活力比标准测定方法提高了20%,在酸性条件下比中性条件下稳定。最后,研究了此β-葡萄糖苷酶和其它商业化的纤维素酶复配对气爆秸秆糖化和同步糖化发酵方面的应用,经过单因子方法设计和统计学分析优化,确定糖化条件为：基质浓度为3.05%、糖化pH值为3.73、糖化温度为43.38℃和酶配比中β-葡萄糖苷酶和纤维素酶的比例为0.91时,糖化率达到88.41%；同步糖化发酵结果证明,添加Novo-188商业化β-葡萄糖苷酶的乙醇产量比不添加β-葡萄糖苷酶的提高了50.4%,比添加同等酶活力的商业化Novo-188β-葡萄糖苷酶的乙醇产量提高了32.9%。添加Syzx4苷酶比不添加苷酶乙醇产量提高了一倍。添加Syzx4生产乙醇的速率方面也明显的优于其它两种反应体系。48h乙醇产量已经接近了17.5g/L,120h连续发酵乙醇产量可以达到23.8g/L。
本研究结果表明无论是在气爆秸秆的糖化过程还是在同步糖化发酵过程中,此β-葡萄糖苷酶都表现出优异的性能,具有广阔的应用前景,证实了从腐败玉米秸秆中分离得到的Tolypocladium cylindrosporum syzx4菌株为开发新型β-葡萄糖苷酶制剂提供了应用基础和理论研究。
A thermoacidophilic P-glucosidase from a newly isolated strain Tolypocladium cylindrosporum syzx4 was purified, characterized and applied to saccharify the corn stover. The enzyme was purified to homogeneity by sulfate precipitataion, diethylaminoethyl cellulose anion exchange chromatography and Sephadex G-100 gel filtration with a 9.47-fold increase in specific activity and 12.27 % recovery. The Mw of the P-glucosidase was 58.6 kDa. Then the following physicochemical and kinetic parameters of theβ-glucosidase were studied respectively:Km, Vmax, Kcat with high affinity p-NPG as the substrate, Ki with the tolerance of glucose and Gluconolactone. Theβ-glucosidase showed highly activity over a wide range of temperature from 35 to 70℃and it was more stable at acidic than neutral pH. The P-glucosidase was activated by Zn2+, Cu2+and Mn2+, while, Ag+and Hg2+inhibited it. The unique enzymatic properties make theβ-glucosidase more effective in the saccharification of steam explosion pretreated corn stover than that from Aspergillus sp. (Novo-188).
1. Production ofβ-glucosidase by a novel isolated strain Tolypocladium cylindrosporum syzx4 and optimization of fermentation medium
A novel fungus, named T. cylindrosporum syzx4, which can efficiently produce extracellularβ-glucosidase, was isolated from naturally rotten corn stover. It is first time to report theβ-glucosidase produced by T. cylindrosporum gams using agro-industrial residues in SmF. The fermentation variables optimized by Single-factor experiment approach were further optimized by statistical optimization. Results of Plackett-Burman design indicated the evaluation of the medium components could be ranked as:TCS> KH2PO4> SM= (NH4)2SO4 With the optimum medium with viz. TCS 26.274 g/L, SM 7.066 g/L, KH2PO4 1.991 g/L, (NH4)2SO4 2.328 g/L predicted by GA-ANN model with others as the original,2.662U/mLβ-glucosidase activity was obtained. With the optimal condition,2.714U/mL P-glucosidase activity was obtaind. Results suggest that the P-glucosidase can be used for various biotechnological applications.
2. Purification ofβ-glucosidase from T. cylindrosporum
All purification processes were conducted at room temperature unless otherwise specified. A clean supernatant with theβ-glucosidase activity of 3300 U was adjusted to 80% saturation by adding solid ammonium sulfate over night. Precipitate was collected by centrifugation at 10000xg for 30min at 4℃and dialyzed against the citrate buffer. Insoluble precipitates were removed by centrifugation, and the supernatant was used for further purification. This step resulted in a 70.3% recovery and 1.38-fold purification. The enzyme was loaded onto a DEAE cellulose column equilibrated with citrate buffer. The elution result of the DEAE cellulose column with a linear gradient of 0-1 moL/L sodium chloride. Two peaks were obtained with one of them showing the P-glucosidase activity. Activity fractions were pooled, concentrated with PEG4000 and dialyzed against citrate buffer. The result showed a total activity of 1488 U,45.1% recovery,5.33-fold purification with the specific activity 19.8 U/mg. The disposed fractions with P-glucosidase activity were then chromatographed on a Sephadex G-100 column pre-equilibrated with citrate buffer. Elution was done with the same buffer, and fractions withβ-glucosidase activity were pooled, dialyzed and concentrated. Theβ-glucosidase ctivity revealed as a single peak through elution. The results showed 12.3 % recovery,9.47-fold purification, a total activity of 405 U and the specificβ-glucosidase activity reached 35.3 U/mg.
3. Characterization of the purified P-glucosidase from T. cylindrosporum
The purified P-glucosidase preparation was examined by SDS-PAGE and Native-PAGE. In SDS-PAGE examination, the purified P-glucosidase was represented by a single band of Mw 58.6 kDa strained with Coomassi blue. The result of Native-PAGE showed that the enzyme reversed the activity of dark halo.
The optimum temperature of the purified enzyme was found to be 60℃, and the purified P-glucosidase activity left 81% and 90% even if it was incubated at 35℃and 70℃, respectively. It is first time for us to report the P-glucosidase with wide temperature adaptability (35-70℃). The purified P-glucosidase had the potential to widely use in various biotechnological applications. Moreover, its maximal activity is at 60℃, which is higer than known P-glucosidases in microorganism in previous reported. The thermal stability results were showed at pH 4.5 incubation in different temperatures. The results indicate that the enzyme with half life about 50 min at 70℃was much more stable than any other (3-glucosidases reported. The enzyme is not stable above 80℃and only 20% activity was reserved for 20min.
The purifiedβ-glucosidase was incubated for various times in buffer with different pH (from 2.0 to 9.0) for 30 min at 37℃. The purified P-glucosidase had an optimum pH around 2.4. The P-glucosidase activity increased markedly with the pH from 1.8 to 2.4, however, it decreased observably while pHs above 2.6. The optimum pH of purifiedβ-glucosidase is lower than that of reported. Interesting, the optimum pH is according to the sulfuric acid for the pretreatment cellulose and steam explosion pretreated cellulose. In addtion, according to the pH stability data, theβ-glucosidase activity retained more than 80 % after being incubated for 12 h at different pH ranged from 3 to 6. The result indicated that P-glucosidase was more stable at acidic pH than neutral pH. The P-glucosidase from T. cylindrosporum, therefore, exhibits a number of highly appealing and promising features, which make it a strong candidate for various biotechnological applications and industrial processes.
The effects of various mental ions and chemical reagents (10 mmol/L) on enzyme activity were examined on p-NPG at pH 4.5 and 37℃. No significant effect was examined in the presence of Mg2+, Ca2+, K+, Fe2+and Ba2+. The P-glucosidase was activated by Zn2+, Cu2+and Mn2+; on the other hand, Ag+and Hg2+had a strong inhibitory effect on the enzyme activity. The P-glucosidase was resistant to 10 mmmol/L SDS with all its activity. However, EDTA, a chelating reagent, and DTT, a disulfide-reducing reagent, were observed to inhibit the enzyme activity, which suggested that the moderate mental ions and the disulfide bonds are essential to maintain the P-glucosidase activity.
Kinetic parameters of the P-glucosidase for p-NPG, salicin or cellobiose were estimated at pH 4.5 and 37℃, respectively.
The Km indicated that theβ-glucosidase had greatest affinity towards p-NPG than others. And the Vmax for p-NPG was much higher than salicin and cellobuose. It may be caused by the structural difference of substrate, as p-NPG and salicin are synthetic aryl P-glucosidase, and cellobiose is the natural substrate. In addition, the Km of salicin is about ten times than that of p-NPG, the reason of which may due to the structural difference of the two arylβ-glucosidases. The Vmax(85.23 mmoL/s) was much higher and the Km (0.85mmol/L) were much lower than P-glucosidase (Novo-188) from A. niger and others when p-NPG was used as a substrate. The effects of glucose (0-100 mmol/L) on p-NPG hydrolyzing activity of theβ-glucosidase were determinated. The inhibition pattern was of the competitive type which was accorded to previous reportes. The hydrolyzing activity decreased markedly with the concentration increasing of glucose. It had an obviously inhibitory effect on p-NPG hydrolyzing activity while the concentration of glucose was above 25.0 mmol/L.
Furthermore, the inhibition constant (Ki) of theβ-glucosidase for glucose was 39.5 mM with p-NPG as a substrate and Ki of Novo-188 with the same condition was 3.0 mM. The Ki of glucose to the purifiedβ-glucosidase was much higher than others reported in literates. The P-glucosidase with the higher concentration tolerance of glucose was very useful for saccharification of lignocellulose.
The effects of gluconolactone (0-200μmol/L) on p-NPG hydrolyzing activity of theβ-glucosidase were determinated. The inhibition pattern was of the competitive type which was accorded to previous reportes. The hydrolyzing activity decreased markedly with the concentration increasing of glucose. It had an obviously inhibitory effect on p-NPG hydrolyzing activity while the concentration of glucose was above 40μmol/L. The inhibition constant (Ki) of theβ-glucosidase for gluconolactone was 13.29μmol/L.
4. Application of P-glucosidase from T. cylindrosporum
After purification and characterization the P-glucosidase, it was applied to saccharify steam explosion pretreated corn stover(SCS) with commercial Celluclast from Trichoderma reesei comparison with theβ-glucosidase(Novo-188) from Aspergillus niger supplementation. Based on the results of single factor tests, further studies with Response Surface Methodology(RSM) with a five level four-factor Central Composite Design(CCD) were used to optimal the hydrolysis parameters such as the concentration of substrate, pH, temperature, the ratio of Celluclast to Syzx4 to achieve the highest saccharification yield. The concentration of substrate and the ratio of Celluclast to Syzx4 were identified as the limiting factor for the saccharification yield. A maximum saccharification yield of 88.4 % was obtained at an the optimal hydrolysis condition as follows:the concentration of substrate 3.05 %, pH 3.73, temperature 43.4℃and the ratio of Syzx4 to Celluclast 0.91(18.2 BGU/g substrate): 1 (20 FPU/g substrate). The results of a confirmation experiment under the optimum conditions agreed well with model predictions and got the maximum value of 88.41 % saccharification yield. The results suggested that theβ-glucosidase(Syzx4) from T. cylindrosporum is a good supplementation for the production of reducing sugars from cellulosic biomass.
In SSF of SCS, three kinds of cellulase mixtures were added to the reaction mixture, respectively,1:Cellulast 20U/g substrate; 2:Cellulast 20U/g substrate and Novo-188 18 U/g substrate; 3:Cellulast 20U/g substrate and Syzx4 18 U/g substrate. The extra 50.4% enthal yield was obtained compared Cellulast 20U/g with the Cellulast 20U/g and Novo-188 18 U/g. The enthal yield of Cellulast 20U/g and Syzx4 18 U/g was 32.9% higher than Cellulast 20U/g and Novo-188. The result indicated that theβ-glucosidase (Syzx4) from T. cylindrosporum was more effective than Novo-188 in the SSF process. After 48h formenation, the ethanol concentration was 17.5%. With the help of the high concentration tolerance of glucose forβ-glucosidase from T. cylindrosporum and other excellent enzymatic parametics make the P-glucosidase (Syzx4) potential application in the saccharification of steam explosion pretreated corn stover for ethanol production.
首先,使用Plackett-Burmans实验设计法对碳源、氮源和无机盐进行产酶显著性的分析,培养基组分对β-葡萄糖苷酶生产影响排序为：TCS>KH2PO4> SM=(NH4)2SO4;然后应用计算机辅助模型拟合的方法对培养基进行进一步的优化,建立的模型包括响应面法和人工智能,人工智能模型表现的非常优异,得到的最佳培养基组成为：TCS 26.274 g/L,SM 7.066 g/L, KH2PO41.991 g/L, (NH4)2SO42.328 g/L,其它成分保持原始值,30℃,初始pH值为5时,发酵8天,此时发酵生产的β-葡萄糖苷酶活力可以达到2.714U/mL。
接下来对Tolypocladium cylindrosporum syzx4发酵生产的β-葡萄糖苷酶进行纯化、性质分析、糖化和同步糖化发酵气爆玉米秸秆的应用研究。酶的纯化过程采用的是硫酸铵沉淀法,DEAE-52纤维素离子交换法和Sephadex G-100凝胶层析法。纯化后相对于纯化前的粗酶液活力提高了9.47倍,回收率为12.27%,得到的酶活力为40.50U/mL。SDS-PAGE结果显示为分子量为58.6 kDa的一条带,表明达到了电泳纯,Native-PAGE的结果表明此β-葡萄糖苷酶表现出良好的生物活性。酶学性质分析以β-葡萄糖苷酶对常用的三种水解底物为对象即纤维二糖,水杨素和p-NPG,研究了酶的水解性质,水杨素为底物时Km为8.8 mmoL/L Vmax为25.6 mmoL/s和Kcat为53.89 s-1；以纤维二糖为底物时得到Km为2.59mmoL/L、Vmax为45.3 mmoL/s和Kcat为95.37s-1；对硝基苯-β-D葡萄糖苷(p-NPG)为底物时得到Km为0.85 mmoL/Lmax为85.23 mmoL/s和Kcat为179.43s-1；以p-NPG为底物时,酶对葡萄糖的抑制常数Ki为3.95 mmoL/L,对葡萄糖醛酸内酯的抑制常数Ki为13.29μmol/L,β-葡萄糖苷水解酶具有较强的耐受葡萄糖和葡萄糖醛酸内酯的的性能,温度和pH值对酶活性的影响分析表明广泛的温度适应性在35到70℃反应时酶活性保留了85%以上；该酶耐酸性很强,在pH值为3.0时活力比标准测定方法提高了20%,在酸性条件下比中性条件下稳定。最后,研究了此β-葡萄糖苷酶和其它商业化的纤维素酶复配对气爆秸秆糖化和同步糖化发酵方面的应用,经过单因子方法设计和统计学分析优化,确定糖化条件为：基质浓度为3.05%、糖化pH值为3.73、糖化温度为43.38℃和酶配比中β-葡萄糖苷酶和纤维素酶的比例为0.91时,糖化率达到88.41%；同步糖化发酵结果证明,添加Novo-188商业化β-葡萄糖苷酶的乙醇产量比不添加β-葡萄糖苷酶的提高了50.4%,比添加同等酶活力的商业化Novo-188β-葡萄糖苷酶的乙醇产量提高了32.9%。添加Syzx4苷酶比不添加苷酶乙醇产量提高了一倍。添加Syzx4生产乙醇的速率方面也明显的优于其它两种反应体系。48h乙醇产量已经接近了17.5g/L,120h连续发酵乙醇产量可以达到23.8g/L。
本研究结果表明无论是在气爆秸秆的糖化过程还是在同步糖化发酵过程中,此β-葡萄糖苷酶都表现出优异的性能,具有广阔的应用前景,证实了从腐败玉米秸秆中分离得到的Tolypocladium cylindrosporum syzx4菌株为开发新型β-葡萄糖苷酶制剂提供了应用基础和理论研究。
A thermoacidophilic P-glucosidase from a newly isolated strain Tolypocladium cylindrosporum syzx4 was purified, characterized and applied to saccharify the corn stover. The enzyme was purified to homogeneity by sulfate precipitataion, diethylaminoethyl cellulose anion exchange chromatography and Sephadex G-100 gel filtration with a 9.47-fold increase in specific activity and 12.27 % recovery. The Mw of the P-glucosidase was 58.6 kDa. Then the following physicochemical and kinetic parameters of theβ-glucosidase were studied respectively:Km, Vmax, Kcat with high affinity p-NPG as the substrate, Ki with the tolerance of glucose and Gluconolactone. Theβ-glucosidase showed highly activity over a wide range of temperature from 35 to 70℃and it was more stable at acidic than neutral pH. The P-glucosidase was activated by Zn2+, Cu2+and Mn2+, while, Ag+and Hg2+inhibited it. The unique enzymatic properties make theβ-glucosidase more effective in the saccharification of steam explosion pretreated corn stover than that from Aspergillus sp. (Novo-188).
1. Production ofβ-glucosidase by a novel isolated strain Tolypocladium cylindrosporum syzx4 and optimization of fermentation medium
A novel fungus, named T. cylindrosporum syzx4, which can efficiently produce extracellularβ-glucosidase, was isolated from naturally rotten corn stover. It is first time to report theβ-glucosidase produced by T. cylindrosporum gams using agro-industrial residues in SmF. The fermentation variables optimized by Single-factor experiment approach were further optimized by statistical optimization. Results of Plackett-Burman design indicated the evaluation of the medium components could be ranked as:TCS> KH2PO4> SM= (NH4)2SO4 With the optimum medium with viz. TCS 26.274 g/L, SM 7.066 g/L, KH2PO4 1.991 g/L, (NH4)2SO4 2.328 g/L predicted by GA-ANN model with others as the original,2.662U/mLβ-glucosidase activity was obtained. With the optimal condition,2.714U/mL P-glucosidase activity was obtaind. Results suggest that the P-glucosidase can be used for various biotechnological applications.
2. Purification ofβ-glucosidase from T. cylindrosporum
All purification processes were conducted at room temperature unless otherwise specified. A clean supernatant with theβ-glucosidase activity of 3300 U was adjusted to 80% saturation by adding solid ammonium sulfate over night. Precipitate was collected by centrifugation at 10000xg for 30min at 4℃and dialyzed against the citrate buffer. Insoluble precipitates were removed by centrifugation, and the supernatant was used for further purification. This step resulted in a 70.3% recovery and 1.38-fold purification. The enzyme was loaded onto a DEAE cellulose column equilibrated with citrate buffer. The elution result of the DEAE cellulose column with a linear gradient of 0-1 moL/L sodium chloride. Two peaks were obtained with one of them showing the P-glucosidase activity. Activity fractions were pooled, concentrated with PEG4000 and dialyzed against citrate buffer. The result showed a total activity of 1488 U,45.1% recovery,5.33-fold purification with the specific activity 19.8 U/mg. The disposed fractions with P-glucosidase activity were then chromatographed on a Sephadex G-100 column pre-equilibrated with citrate buffer. Elution was done with the same buffer, and fractions withβ-glucosidase activity were pooled, dialyzed and concentrated. Theβ-glucosidase ctivity revealed as a single peak through elution. The results showed 12.3 % recovery,9.47-fold purification, a total activity of 405 U and the specificβ-glucosidase activity reached 35.3 U/mg.
3. Characterization of the purified P-glucosidase from T. cylindrosporum
The purified P-glucosidase preparation was examined by SDS-PAGE and Native-PAGE. In SDS-PAGE examination, the purified P-glucosidase was represented by a single band of Mw 58.6 kDa strained with Coomassi blue. The result of Native-PAGE showed that the enzyme reversed the activity of dark halo.
The optimum temperature of the purified enzyme was found to be 60℃, and the purified P-glucosidase activity left 81% and 90% even if it was incubated at 35℃and 70℃, respectively. It is first time for us to report the P-glucosidase with wide temperature adaptability (35-70℃). The purified P-glucosidase had the potential to widely use in various biotechnological applications. Moreover, its maximal activity is at 60℃, which is higer than known P-glucosidases in microorganism in previous reported. The thermal stability results were showed at pH 4.5 incubation in different temperatures. The results indicate that the enzyme with half life about 50 min at 70℃was much more stable than any other (3-glucosidases reported. The enzyme is not stable above 80℃and only 20% activity was reserved for 20min.
The purifiedβ-glucosidase was incubated for various times in buffer with different pH (from 2.0 to 9.0) for 30 min at 37℃. The purified P-glucosidase had an optimum pH around 2.4. The P-glucosidase activity increased markedly with the pH from 1.8 to 2.4, however, it decreased observably while pHs above 2.6. The optimum pH of purifiedβ-glucosidase is lower than that of reported. Interesting, the optimum pH is according to the sulfuric acid for the pretreatment cellulose and steam explosion pretreated cellulose. In addtion, according to the pH stability data, theβ-glucosidase activity retained more than 80 % after being incubated for 12 h at different pH ranged from 3 to 6. The result indicated that P-glucosidase was more stable at acidic pH than neutral pH. The P-glucosidase from T. cylindrosporum, therefore, exhibits a number of highly appealing and promising features, which make it a strong candidate for various biotechnological applications and industrial processes.
The effects of various mental ions and chemical reagents (10 mmol/L) on enzyme activity were examined on p-NPG at pH 4.5 and 37℃. No significant effect was examined in the presence of Mg2+, Ca2+, K+, Fe2+and Ba2+. The P-glucosidase was activated by Zn2+, Cu2+and Mn2+; on the other hand, Ag+and Hg2+had a strong inhibitory effect on the enzyme activity. The P-glucosidase was resistant to 10 mmmol/L SDS with all its activity. However, EDTA, a chelating reagent, and DTT, a disulfide-reducing reagent, were observed to inhibit the enzyme activity, which suggested that the moderate mental ions and the disulfide bonds are essential to maintain the P-glucosidase activity.
Kinetic parameters of the P-glucosidase for p-NPG, salicin or cellobiose were estimated at pH 4.5 and 37℃, respectively.
The Km indicated that theβ-glucosidase had greatest affinity towards p-NPG than others. And the Vmax for p-NPG was much higher than salicin and cellobuose. It may be caused by the structural difference of substrate, as p-NPG and salicin are synthetic aryl P-glucosidase, and cellobiose is the natural substrate. In addition, the Km of salicin is about ten times than that of p-NPG, the reason of which may due to the structural difference of the two arylβ-glucosidases. The Vmax(85.23 mmoL/s) was much higher and the Km (0.85mmol/L) were much lower than P-glucosidase (Novo-188) from A. niger and others when p-NPG was used as a substrate. The effects of glucose (0-100 mmol/L) on p-NPG hydrolyzing activity of theβ-glucosidase were determinated. The inhibition pattern was of the competitive type which was accorded to previous reportes. The hydrolyzing activity decreased markedly with the concentration increasing of glucose. It had an obviously inhibitory effect on p-NPG hydrolyzing activity while the concentration of glucose was above 25.0 mmol/L.
Furthermore, the inhibition constant (Ki) of theβ-glucosidase for glucose was 39.5 mM with p-NPG as a substrate and Ki of Novo-188 with the same condition was 3.0 mM. The Ki of glucose to the purifiedβ-glucosidase was much higher than others reported in literates. The P-glucosidase with the higher concentration tolerance of glucose was very useful for saccharification of lignocellulose.
The effects of gluconolactone (0-200μmol/L) on p-NPG hydrolyzing activity of theβ-glucosidase were determinated. The inhibition pattern was of the competitive type which was accorded to previous reportes. The hydrolyzing activity decreased markedly with the concentration increasing of glucose. It had an obviously inhibitory effect on p-NPG hydrolyzing activity while the concentration of glucose was above 40μmol/L. The inhibition constant (Ki) of theβ-glucosidase for gluconolactone was 13.29μmol/L.
4. Application of P-glucosidase from T. cylindrosporum
After purification and characterization the P-glucosidase, it was applied to saccharify steam explosion pretreated corn stover(SCS) with commercial Celluclast from Trichoderma reesei comparison with theβ-glucosidase(Novo-188) from Aspergillus niger supplementation. Based on the results of single factor tests, further studies with Response Surface Methodology(RSM) with a five level four-factor Central Composite Design(CCD) were used to optimal the hydrolysis parameters such as the concentration of substrate, pH, temperature, the ratio of Celluclast to Syzx4 to achieve the highest saccharification yield. The concentration of substrate and the ratio of Celluclast to Syzx4 were identified as the limiting factor for the saccharification yield. A maximum saccharification yield of 88.4 % was obtained at an the optimal hydrolysis condition as follows:the concentration of substrate 3.05 %, pH 3.73, temperature 43.4℃and the ratio of Syzx4 to Celluclast 0.91(18.2 BGU/g substrate): 1 (20 FPU/g substrate). The results of a confirmation experiment under the optimum conditions agreed well with model predictions and got the maximum value of 88.41 % saccharification yield. The results suggested that theβ-glucosidase(Syzx4) from T. cylindrosporum is a good supplementation for the production of reducing sugars from cellulosic biomass.
In SSF of SCS, three kinds of cellulase mixtures were added to the reaction mixture, respectively,1:Cellulast 20U/g substrate; 2:Cellulast 20U/g substrate and Novo-188 18 U/g substrate; 3:Cellulast 20U/g substrate and Syzx4 18 U/g substrate. The extra 50.4% enthal yield was obtained compared Cellulast 20U/g with the Cellulast 20U/g and Novo-188 18 U/g. The enthal yield of Cellulast 20U/g and Syzx4 18 U/g was 32.9% higher than Cellulast 20U/g and Novo-188. The result indicated that theβ-glucosidase (Syzx4) from T. cylindrosporum was more effective than Novo-188 in the SSF process. After 48h formenation, the ethanol concentration was 17.5%. With the help of the high concentration tolerance of glucose forβ-glucosidase from T. cylindrosporum and other excellent enzymatic parametics make the P-glucosidase (Syzx4) potential application in the saccharification of steam explosion pretreated corn stover for ethanol production.
引文
[1]Szczodrak J., Fiedurek J. Technology for conversion of lignocellulosic biomass to ethanol[J]. Biomass and bioenergy,1996,10 (6):367-375.
[2]Kim S, Dale B E. Global potential bioethanol production from wasted crops and crop residues[J]. Biomass and Bioenergy,2004,26:361-375
[3]Hill, J., Nelson, E., Tilman, D., Polasky, S.& Tiffany, D. Environmental, economic, and energetic costs and benefits of biodiesel and ethanol biofuels[M]. Proc. Natl Acad. Sci. USA 2006,103:11206-11210
[4]Kubicek, C.P., Messner, R., Gruber, F., Mach, R.L., and Kubicek-Pranz, E.M.1993. The Trichoderma cellulase regulatory puzzle:from the interior life of a secretory fungus[J]. Enz. Microb. Technol.15:90-99.
[5]Rosi, I., Vinella, M., and Domezio, M.1994. Characterization of β-glucosidase activity in yeasts of enological origin[J]. J. Appl. Bact.77:519-527.
[6]Esen, A. β-glucosidases:overview, in β-Glucosidases:Biochemistry and Molecular Biology[M], Esen, A., Ed., American Chemical Society, Washington, DC,1993:1-14.
[7]Fredrickson, D.S., and Sloan, H.R. The Metabolic Basis of Inherited Disease[M]. (Stanbury, J.B., Wygnaarden, J.B., and Fredrickson, D.S., Eds.) McGraw-Hill, New York,1972:7730.
[8]Henrissat, B. A classification of glycosyl-hydrolases based on amino acid sequence similarities[J]. Biochem. J.1991,293:781-788.
[9]Henrissat, B. and Bairoch, A. Updating the sequence-based classification of glycosyl hydrolases[J]. Biochem. J.1996,316:695-696.
[10]Cantarel BL, Coutinho PM, Rancurel C, Bernard T, Lombard V, Henrissat B. The Carbohydrate-Active EnZymes database (CAZy):an expert resource for glycogenomics[J]. Nucleic Acids Res 2009,37:233-238
[11]Henrissat B. A classification of glycosyl hydrolases based on amino acid sequence similarities[J]. Biochem J 1991,280:309-316
[12]Opassiri R, Pomthong B, Akiyama T, Nakphaichit M, Onkoksoong T, Ketudat-Cairns M, Ketudat Cairns JR A stress-induced rice b-glucosidase represents a new subfamily of glycosyl hydrolase family 5 containing a fascin-like domain[J]. Biochem J 2007,408:241-249
[13]Wohler F., Liebig J. Annu. Pharm.1837,22:1-24
[14]Ander F, Lars R. Expression of azeatin-glucoside-degrading β-glucosidase in Brassicanapus. Plant-Physiolgy(USA) [J],1995,108:1369-1377
[15]Barrett T, Suresh C G. Tolley S P, Dodson E J, Hughes M A. The crystal structure of a cyanogenic B-glucosidase from white clover, a family 1 glycosyl hydrolase[J]. Structure. 1995,3:951-960
[16]Yukti Bhatia, Saroj Mishra, and V.S. Bisaria, Microbial β-Glucosidases:Cloning, Properties, and Applications[J]. Critical Reviews in Biotechnology,2002.22(4):375-407
[17]Sternberg D. (3-Glucosidase of Trichoderma:its biosynthesis and role in saccharification ofcellulose[J].Applied and Environmental Microbiology,1976,31(5):648-654
[18]Awafo V A, Chahal D S, Simpson B K. Evaluation of combination treatments of sodium xyoxide steam explosion for the production of cellulose-systems by two Trichoderma mutants underand solid-state fermentation conditions[J]. Bioresource technology,2000,73(3): 235-245
[19]Tangnu S K, Blanch H W, Wilke C R. Enhanced production of cellulase, hemicellulase and β-glucosidase by Trichoderma reesei[J]. Biotech Bioengin,1981,23,1837-1849
[20]Jianmin Gao, Haibo Weng, Daheng Zhu, Mingxue Yuan, Fangxia Guan, Yu Xi, Production and characterization of cellulolytic enzymes from the thermoacidophilic fungal Aspergillus terreus M11 under solid-state cultivation of corn stover[J]. Bioresource Technology 2008,99: 7623-7629
[21]杨建海,任大明.黑曲霉p-葡萄糖苷酶高产菌株的Co60-52-23的选育[J]，食品与发酵工业,2005，31(6)：147-150
[22]Hida, H., Yamada, T., Yamada, Y., Genome shuffling of Streptomyces sp. U121 for improved production of hydroxycitric acid[J]. Appl. Microbiol. Biotechnol.2007,73: 1387-1393.
[23]Lin, J., Shi, B.H., Shi, Q.Q., He, Y.X., Wang, M.Z.. Rapid improvement in lipase production of Penicillium expansum by genome shuffling[J]. Chin. J. Biotechnol.2007,23:672-676.
[24]Yao, Q., Sun, T.T., Liu, W.F., Chen, G.J., Gene cloning and heterologous expression of a novel endoglucanase, swollenin, from Trichoderma pseudokoningii S38[J]. Biosci. Biotechnol. Biochem.2008,72:2799-2805.
[25]Fengchao Wang, Fan Li, Guanjun Chen, Weifeng Liiu. Isolation and characterization of novel cellulase genes from uncultured microorganisms in different environmental niches[J], Microbiological Research,2009,164(6):650-657.
[26]Philip Hugenholtz and Gene W. Tyson, Metagenomics, nature,2008,455(25),481-483
[27]Susannah Green Tringe and Edward M. Rubin, Metagenomics DNA sequencing of environmental samples[J], nature reviews genetics,2005,6:805-814
[28]Nathan Blow. Exploring unseen communities, Technology feature metagenomics[J], nature, 2008,453(29):687-690
[29]E. Kalogeris, P. Christakopoulos, P. Katapodis, A. Alexiou, S. Vlachou, D. Kekos, B.J. Macris Production and characterization of cellulolytic enzymes from the thermophilic fungus Thermoascus aurantiacus under solid state cultivation of agricultural wastes[J]. Process Biochemistry,2003,38:1099-1104
[30]Yejun Han, Hongzhang Chen, Characterization of beta-glucosidase from corn stover and its application in simultaneous saccharification and fermentation[J], Bioresource Technology 2008,99:6081-6087
[31]Butters TD. Gaucher disease[M]. Curr Opin Chem Biol 2007,11:412-418
[32]Dvir H, Harel M, McCarthy AA, Toker L, Silman I, Futerman AH, Sussman JLX-ray structure of human acid-β-glucosidase, the defective enzyme in Gaucher disease[J]. EMBO Rep 2003,4:704-709
[33]Lieberman RL, Wustman BA, Huertas P, Powe AC, Pine CW, Khanna R, Schlossmacher MG, Ringe D, Petsko GAStructure of acid β-glucosidase with pharmacological chaperone provides insight into Gaucher disease[J]. Nat Chem Biol 2007,3:101-107
[34]Matern H, Boermans H, Lottspeich F, Matern S Molecular cloning and expression of human bile acid beta-glucosidase. J Biol Chem 2001,276:37929-37933
[35]Yildiz Y, Matern H, Thompson B, Allegood JC, Warren RL, Ramirez DMO, Hammer RE, Hamra FK, Matern S, Russell DW beta-Glucosidases Mutation of b-glucosidase 2 causes glycolipid storage disease and impaired male fertiliry[J]. J Clin Invest 2006,116:2985-2994
[36]Boot RG, Verhoek M, Donker-Koopman W, Strijland A, van Marie J, Overkleeft HS, Wennekes T, Aerts JM Identification of the non-lysosomal glucosylceramidase as betaglucosidase 2[J]. J Biol Chem 2007,282:1305-1312
[37]Hayashi Y, Okino N, Kakuta Y, Shikanai T, Tani M, Narimatsu H, Ito M Klotho-related protein is a novel cytosolic neutral β-glycosylceramidase[J]. J Biol Chem 2007,282: 30889-30900
[38]Day AJ, DuPont MS, Ridley S, Rhodes M, Rhodes MJ, Morgan MR, Williamson G Deglycosylation of flavonoid and isoflavonoid glycosides by human small intestine and liver β-glucosidase activity[J]. FEBS Lett 1998,436:71-75
[39]Berrin J-G, McLauchlan WR, Needs P, Williamson G, Puigserver A, Kroon PA, Juge N Functional expression of human liver cytosolic β-glucosidase in Pichia pastoris. Insights into its role in the metabolism of dietary glucosides[J]. Eur J Biochem 2002,269:249-258
[40]Zagrobelny M, Bak S, M(?)ller BL Cyanogenesis in plants and arthropods [J]. Phytochemistry 2008,69:1457-1468
[41]Ferrieira AHP, Marana SR, Terra WR, Ferreira C Purification, molecular cloning, and properties of a b-glycosidase isolated from midgut lumen of Tenebrio molitor (Coleoptera) larvae[J]. Insect Biochem Mol Biol 2001,31:1065-1076
[42]Jones AME, Bridges M, Bones AM, Cole R, Rossiter JT Purification and characterisation of a non-plant myrosinase from the cabbage aphid Brevicoryne brassicae[J]. Insect Biochem Mol Biol 2001,31:1-5
[43]Marana SR, Jacobs-Lorena M, Terra WR, Ferrieira C Amino acid residues involved in substrate binding and catalysis in an insect digestive β-glycosidase[J]. Biochim Biophys Acta 2001,1545:41-52
[44]Malboobi MA. Lefebvre D. A phosphate-starvation inducible β-glucosidase gene (psr3.2) isolated from Arabidopsis thaliana is a member of a distinct subfamily of the BGA family[J]. Plant Mol Biol 1997,34:57-68
[45]van de Ven WT, LeVesque CS, Perring TM, Walling LL Local and systemic changes in squash gene expression in response to silver winged whitefly feeding[J]. Plant Cell 2000, 12:1409-1423
[46]Xu Z, Escamilla-Trevino LL, Zeng L, Lalgondar M, Bevan DR, Winkel BSJ, Mohamed A, Cheng C, Shih M, Poulton JE, Esen A Functional genomic analysis of Arabidopsis thaliana glycoside hydrolase family 1[J]. Plant Mol Biol 2004,55:343-367
[47]Opassiri R, Pomthong B, Okoksoong T, Akiyama T, Esen A, Ketudat Cairns JR Analysis of rice glycosyl hydrolase family 1 and expression of Os4bglul2 β-glucosidase[J]. BMC Plant Biol 2006,6:33
[48]Thorlby G, Fourier N, Warren G. The SENSITIVE TO FREEZING2 gene, required for freezing tolerance in Arabidopsis thaliana, encodes a beta-glucosidase[J]. Plant Cell 2004, 16:2192-2203
[49]Marques AR, Coutinho PM, Videira P, Fialho AM, S-Correia I Sphingomonas paucimobilis beta-glucosidase Bgll:a member of a new bacterial subfamily in glycoside hydrolase family 1[J]. Biochem J 2003,370:793-804
[50]Niemeyer HM Hydroxamic acids (4-hydroxy-l,4-benzoxazin-3-ones), defense chemicals in the Gramineae[J]. Phytochemistry 1988,27:3349-3358
[51]Poulton JE Cyanogenesis in plants[J]. Plant Physiol 1990,94:401-405
[52]Morant AV, J(?)gensen K, Jorgensen C, Paquette SM, Sa'nche'z-Perez R, Moller BL, Bak S b-Glucosidases as detonators of plant chemical defense[J]. Phytochemistry 2008, 69:1795-1813
[53]Sherameti I, Venus Y, Drzewiecki C, Tripathi W, Dan VM, Nitz I, Varma A, Grundler F, Oelmu"ller R PYK10, a b-glucosidase located in the endoplasmatic reticulum, is crucial for the beneficial interaction between Arabidopsis thanliana and the endophytic fungus Piriformospora indica[J]. Plant J 2008,54:428-439
[54]Hrmova M, Harvey AJ, Wang J, Shirley NJ, Jones GP, Stone BA, Hoj PB, Fincher GB Barley beta-D-glucan exohydrolases with β-D-glucosidase activity[J]. J Biol Chem 1996, 271:5277-5286
[55]Hrmova M, MacGregor EA, Biely P, Stewart RJ, Fincher GB Substrate binding and catalytic mechanism of a barleyβ-D-glucosidase/(1,4)-β--D-glucan exohydrolase[J]. J Biol Chem 1998,273:11134-11143
[56]Hrmova M, Burton RA, Biely P, Lahnstein J, Fincher GB Hydrolysis of (1,4)-β-D-mannans in barley (Hordeum vulgare L.) is mediated by the concerted action of (1,4)-β-D-mannan endohydrolase and β-D-mannosidase[J]. Biochem J 2006,399:77-90
[57]Akiyama T, Kaku H, Shibuya N. A cell wall-bound b-glucosidase from germinated rice: purification and properties[J]. Phytochemistry 1998,48:49-54
[58]Opassiri R, Ketudat Cairns JR, Akiyama T, Wara-Aswapati O, Svasti J, Esen A Characterization of a rice b-glucosidase highly expressed in flower and germinating shoot[J]. Plant Sci 2003,165:627-638
[59]Opassiri R, Hua Y, Wara-Aswapati O, Akiyama T, Svasti J, Esen A, Ketudat Cairns JR beta-Glucosidase, exo-beta-glucanase and pyridoxine transglucosylase activities of rice BGlul[J]. Biochem J 2004,379:125-131
[60]Seshadri S, Akiyama T, Opassiri R, Kuaprasert B, Ketudat Cairns J Structural and enzymatic characterization ofOs3BGlu6, a rice b-glucosidase hydrolyzing hydrophobic glycosides and (1-3)-and (1-2)-linked disaccharides[J]. Plant Physiol 2009,151:47-58
[61]Hosel W, Surholt E, Borgmann E Characterization of b-glucosidase isoenzymes possibly involved in lignification from chick pea (Cicer arietinum L.) cell suspension culture[J]. Eur J Biochem 1978,84:487-492
[62]Schliemann W Hydrolysis of conjugated gibberellins by beta-glucosidases from dwarf rice (Oryza sativa L. cv. Tan-ginbozu) [J]. J Plant Physiol 1984,116:123-132
[63]Brzobohaty'B, Moore I, Kristoffersen P, Bako L, Campos N, Schell J, Palme K Release of active cytokinin by a β-glucosidase localized to the maize root meristem[J]. Science 1993, 262:1051-1054
[64]Dietz K-J, Sauter A, Wichert K, Messdaghi D, Hartung W Extracellular b-glucosidase activity in barley involved in the hydrolysis of ABA glucose conjugate in leaves[J]. J Exp Bot 2000,51:937-944
[65]Jakubowska A, Kawalczyk S A specific enzyme hydrolyzing 6-0(4-0)-indole-3-ylacetyl-β-D-glucose in immature kernels of Zea mays[J]. J Plant Physiol 2005,162:207-213
[66]Crout DH, Vic G Glycosidases and glycosynthetases in intermediate in the biosynthesis of monoterpenoid indole alka-glycoside and oligosaccharide synthesis[J]. Curr Opin Chem Biol loids. J Chem Soc Chem Commun 1998:98-111
[67]Barleben L, Panjikar S, Ruppert M, Koepke J, Sto'ckigt J Henrissat B, Callebaut I, Fabrega S, Lehn P, Mornon JP, Davies Molecular architecture of strictosidine glucosidase:the gateway G Conserved catalytic machinery and the prediction of a to the biosynthesis of the monoterpenoid indole alkaloid family. Common fold for several families of glycosyl hydrolases. Proc Plant Cell 19:2886-2897 Natl Acad Sci USA 92:7090-7094
[68]Jenkins J, Lo Leggio L, Harris G, Pickersgill R., Beta-Molecular cloning and functional bacterial expression of a plant glucosidase, beta-galactosidase, family A cellulases, family F β-glucosidase specifically involved in alkaloid biosynthesis. xylanases and two barley glycanases form a superfamily of Phytochemistry[M].1995,54:657-666
[69]Nomura T, Quesada AL, Kutchan TM. The new beta-D-glucosidase in terpenoid isoquinoline alkaloid biosynthesis in Psychotria ipecacuanha[J]. J Biol Chem 2008, 283:34650-34659
[70]Reuveni M, Sagi Z, Evnor D, Hetzroni A b-Glucosidase activity is involved in scent production in Narcissus flowers[J]. Plant Sci 1999,147:19-24
[71]Mattiacci L, Dicke M, Posthumus MA Beta-glucosidase:an elicitor of herbivore-induced plant odor that attracts host-searching parasitic wasps[J]. Proc Natl Acad Sci USA 1995, 92:2036-2040
[72]Gilbert HJ, Brumer H How the walls come tumbling down:recent structural biochemistry of plant poly-saccharide degradation[J]. Curr Opin Plant Biol 2008,11:338-348
[73]Doi RH, Kosugi A Cellulosomes:plant-cell-wall-degrading enzyme complexes[J]. Nat Rev Microbiol 2004,2:541-551
[74]Carvalho AL, Dias FM, Nagy T, Prates JA, Proctor MR, Smith N, Bayer EA, Davies GJ, Ferreira LM, Roman?oMJ, Fontes CM, Gilbert HJ., Evidence for a dual binding mode of dockerin modules to cohesins[J]. Proc Natl Acad Sci USA 2007(104):3089-3094
[75]Lymar ES, Li B, Renganathan V. Purification and characterization of a cellulose-binding β-glucosidase from cellulose degrading cultures of Phanerochaete chrysosporium[J]. Appl Environ Microbiol 1995,61:2976-2980
[76]Igarashi K, Tani T, Kawal R, Samejima M Family 3 b-glucosidase from cellulose-degrading culture of the white-rot fungus Phanerochaete chrysosporium[J], J Biosci Bioeng 2003, 95:572-576
[77]Henrissat B, Callebaut I, Fabrega S, Lehn P, Mornon JP, Davies G Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases[J]. Proc Natl Acad Sci USA 1995,92:7090-7094
[78]Jenkins J, Lo Leggio L, Harris G, Pickersgill R Beta-glucosidase, beta-galactosidase, family A cellulases, family F xylanases and two barley glycanases form a superfamily of enzymes with 8-fold beta/alpha architecture and with two conserved glutamates near the carboxy-terminal ends of beta strands four and seven[J]. FEBS Lett 1995,362:281-285
[79]Sanz-Aparicio J, Hermoso JA, Martinez-Ripoll M, Lequerica JL, Polaina J Crystal structure of beta-glucosidase A from Bacillus polymyxa:insights into the catalytic activity in family 1 glycosyl hydrolases[J]. J Mol Biol 1998,275:491-502
[80]Varghese J N, Hrmova M, FincherGBThree-dimensional structure of a barley β-D-glucan exohydrolase; a family 3 glycosyl hydrolase[J]. Structure 1999,7:179-190
[81]Hrmova M, Varghese JN, De Gori R, Smith BJ, Driguez H, Fincher GB Catalytic mechanisms and reaction intermediates along the hydrolytic pathway of a plant β-D-glucan glucohydrolase[J]. Structure 2001,9:1005-1016
[82]Park JK, Wang L-X, Patel HV, Roseman S Molecular cloning and characterization of a unique β-glucosidase from Vibrio cholorae[J]. J Biol Chem 2002,277:29555-29560
[83]Qi M, Jun H-S,Forsbert CW., Ce19D,anatypical 1,4-β-D-glucan glucohydrolase from Fibrobacter succinogenes:characteristics, catalytic residues, and synergistic interactions with other cellulases[J]. J Bacteriol 2008,109:1976-1984
[84]Gracia Gonza'lez-Blasco, Juliana Sanz-Aparicio§, Beatriz Gonza'lez, Juan A. Hermoso, Julio Polaina, Directed Evolution of beta-Glucosidase A from Paenibacillus polymyxa to Thermal Resistance[J], The Jouranl of Biological Chemistry 2000,18(5):13708-13712
[85]Davies GJ, Ducros VM-A, Varrot A, Zechel DL Mapping the conformational itinerary of beta-glucosidases by X-ray crystallography [J]. Biochem Soc Trans 2003,31:523-527
[86]Czjzek M, Cicek M, Zamboni V, Bevan DR, Henrissat B, Esen A The mechanism of substrate (aglycone) specificity in b-glucosidases is revealed by crystal structures of mutant maize β-glucosidase-DIMBOA,-DIMBOAGlc, and dhurrin complexes[J]. Proc Natl Acad Sci USA 2000,97:13555-13560
[87]Bauer M W, Kelly R M. The family β--glucosidases from Pyrococcus furiosus and Agrobacterium faecalis share a common catalytic mechanism[J]. Biochemistry,1998,37: 17170-17178
[88]Zechel DL, Boraston AB, Gloster TM, Boraston CM, Macdonald JM, Tilbrook DMG, Stick RV, Davies GJ Iminosugar glycosidase inhibitors:structural and thermodynamic dissection of the binding of isofagomine and 1-deoxynojirimycin to β-glucosidases[J]. J Am Chem Soc 2003,125:14313-14323
[89]Vincent F, Gloster TM, Macdonald J, Morland C, Stick RV, Dias FM, Prates JA, Fontes CM, Gilbert HJ, Davies GJ Common inhibition of both beta-glucosidases and betamannosidases by isofagomine lactam reflects different hydrolysis [J]. Chembiochem 2004,5:1596-1599
[90]Gloster TM, Macdonald JM, Tarling CA, Stick RV, Withers SG, Davies GJ Structural, thermodynamic, and kinetic analyses of tetrahydroozazine-derived inhibitors bound to beta-glucosidases[J]. J Biol Chem 2004,279:29236-49242
[91]Ly HD, Withers SG Mutagenesis of glycosidases. Annu Rev Biochem 1999,68:487-522
[92]Marana SR Molecular basis of substrate specificity in family 1 glycoside hydrolases[J]. IUBMB Life 2006,58:63-73
[93]Verdoucq L, Czjzek M, Moriniere J, Bevan DR. Esen A Mutational and structural analysis of aglycone specificity in maize and sorghum beta-glucosidases[J]. J Biol Chem 2003, 278:25055-25062
[94]Berrin J-G, Czjzek M, Kroon PA, McLauchlan WR, Puigserver A, Williamson G. Juge N Substrate (aglycone) specificity of human cytosolic bete-glucosidase[J]. Biochem J 2003, 373:41-48
[95]Cicek M, Blanchard D, Bevan DR, Esen A The aglycone specificity-determining sites are different in 2,4-dihydroxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA)-glucosidase (maize beta-glucosidase) and dhurrinase (sorghum beta-glucosidase) [J]. J Biol Chem 2000,275: 20002-20011
[96]刘望夷,祁国荣.真核生物核糖体RNA基因的结构与表达[M].北京：科学出版社,1989：46-94
[97]Srisomsap C, Svasti J, Surarit R, Champattanachai V, Sawangareetrakul P, Boonpuan K, Subhasitanont P, Chokchaichamnankit D Isolation and characterization of an enzyme with beta-glucosidase and beta-fucosidase activities from Dalbergia cochinchinensis Pierre[J]. J Biochem 1996,119:585-590
[98]Gloster TM, Meloncelli P, Stick RV, Zechel D, Vasella A, Davies GJ Glycosidase inhibition: an assessment of the binding of 18 putative transition-state mimics[J]. J Am Chem Soc 2007, 129:2345-2354
[99]Zollner H., Handbook of enzyme inhibitors[M]. VCH, Weinheim,1989:94-95
[100]Burmeister WP, Cottaz S, Rollin P, Vasella A, Henrissat B High resolution X-ray crystallography shows that ascorbate is a cofactor for myrosinase and substitutes for the function of the catalytic base[J]. J Biol Chem 2000,275:39385-39393
[101]Nam KH. Kim S-J, Kim M-Y, Kim JH, Yeo Y-S, Lee C-M, Jun H-K, Hwang KY Crystal structure of engineered beta-glucosidase from soil metagenome[J]. Proteins 2008, 73:788-793
[102]Chi YI, Martinez-Cruz LA, Jancarik J, Swanson RV, Robertson DE, Kim SH Crystal structure of the beta-glycosidase from the hyperthermophile Thermosphaera aggregans: insights into its activity and thermostability[J]. FEBS Lett 1999,445:375-383
[103]Yin, J., Liu, D., Strategic thinking on developing petroleum substitutes in China[J]. Petroleum Sci.2006,3:46-51.
[104]Rass-Hansen, J., Falsig, H., Jorgensen, B., Christensen, C.H., Bioethanol:fuel or feedstock? [J], J. Chem. Technol. Biotechnol.2007,82:329-333.
[105]Qu, Y.B., Zhu, M.T., Liu, K., Bao, X.M., Lin, J.Q., Studies on cellulosic ethanol production for sustainable supply of liquid fuel in China[J]. Biotechnol. J.2006,1: 1235-1240
[106]Sanchez, J., Jiang, J.,2008. China, People's Republic of:Bio-fuels annual 2008[J]. USDA, FAS. Gain Report Number CH8052.
[107]Li, S.Z., Chan-Halbrendt, C., Ethanol production in China:potential and technologies[J]. Appl. Energy 2009,4:4-9.
[108]Yang, B., Lu, Y., The promise of cellulosic ethanol production in China[J]. J. Chem. Technol. Biotechnol.2007,82:6-10.
[109]Qu, Y.B., Zhu, M.T., Liu, K., Bao, X.M., Lin, J.Q., Studies on cellulosic ethanol production for sustainable supply of liquid fuel in China[J]. Biotechnol. J.2006,1:1235-1240
[110]Zhang, S.P., Yan, Y.J., Ren, Z.W., Li, T.C., Fuel ethanol production from lignocellulosic biomass[J]. Prog. Chem. (Chinese) 2007,19:1129-1133.
[111]Yao, R.S., Qi, B.K., Deng, S.S., Liu, N., Peng, S.C., Cui, Q.F., Use of surfactants in enzymatic hydrolysis of rice straw and lactic acid production from rice straw by simultaneous saccharification and fermentation[J]. Bioresour.2007,2:389-398.
[112]Shen, Y., Zhang, Y., Ma, T., Bao, X.M., Du, F.G., Zhuang, G.Q., Qu, Y.B., Simultaneous saccharification and fermentation of acid-pretreated corncobs with a recombinant Saccharomyces cerevisiae expressing beta-glucosidase[J]. Bioresour. Technol.2008,99: 5099-5103.
[113]Wyman, C.E., What is (and is not) vital to advancing cellulosic ethanol[J]. Trends Biotechnol.2007,25:153-157.
[114]Gruno, M., Valjamae, P., Pettersson, G., Johansson, G., Inhibition of the Trichoderma reesei cellulases by cellobiose is strongly dependent on the nature of the substrate[J]. Biotechnol. Bioeng.2004,86:503-511
[115]Hou, J., Shen, Y., Li, X.P., Bao, X.M., Effect of the reversal of coenzyme specificity by expression of mutated Pichia stipitis xylitol dehydrogenase in recombinant Saccharomyces cerevisiae[J]. Lett. Appl. Microbiol.2007,45:184-189.
[116]Galbe, M., Zacchi, G., Pretreatment of lignocellulosic materials for efficient bioethanol production[J]. Adv. Biochem. Eng. Biotechnol.2007,108:41-65.
[117]Sanchez, C., Lignocellulosic residues:biodegradation and bioconversion by fungi[J]. Biotechnol. Adv.2009,27:185-194.
[118]Ma, H., Liu, W.W., Chen, X., Wu, Y.J., Yu, Z.L., Enhanced enzymatic saccharification of rice straw by microwave pretreatment[J]. Bioresour. Technol.2009,100:1279-1284.
[119]Chen, H., Han, Y., Xu, J., Simultaneous saccharification and fermentation of steam exploded wheat straw pretreated with alkaline peroxide[J]. Process Biochem.2008,43: 1462-1466.
[120]Cheng, K., Cai, B., Zhang, J., Ling, H., Zhou, Y., Ge, J., Xu, J., Sugarcane bagasse hemicellulose hydrolysate for ethanol production by acid recovery process[J]. Biochem. Eng. J.2008,38:105-109.
[121]Li, L., Li, X.Z., Tang, W.Z., Zhao, J., Qu, Y.B., Screening of a fungus capable of powerful and selective delignification on wheat straw[J]. Lett. Appl. Microbiol.2008,47: 415-420.
[122]Sun, Y., Cheng, J., Hydrolysis of lignocellulosic materials for ethanol production:a review[J]. Bioresour. Technol.2002,83:1-11.
[123]Jing, X.Y., Zhang, X.X., Bao, J., Inhibition performance of lignocellulose degradation products on industrial cellulase enzymes during cellulose hydrolysis[J]. Appl. Biochem. Biotechnol.2009,87:34-40.
[124]Liu, K., Lin, X., Yue, J., Li, X., Fang, X., Zhu, M., Lin, J., Qu, Y., Xiao, L., High concentration ethanol production from corncob residues by fed-batch strategy[J]. Bioresour. Technol.,2009,83:81-87.
[125]Zhao, X., Cheng, K., Liu, D., Organosolv pretreatment of lignocellulosic biomass for enzymatic hydrolysis[J]. Appl. Microbiol. Biotechnol.2009,82:815-827.
[126]Zhu, S.D., Wu, Y.X., Yu, Z.N., Liao, J.T., Zhang, Y., Pretreatment by microwave/alkali of rice straw and its enzymic hydrolysis[J]. Process Biochem.2005,40:3082-3086.
[127]Zeng, W., Chen, H., Synergistic effect of feruloyl esterase and cellulase in hydrolyzation of steam-exploded rice straw[J]. Chin. J. Biotechnol.2009,25:49-54
[128]Kumar, R., Wyman, C.E., Effect of xylanase supplementation of cellulase on digestion of corn stover solids prepared by leading pretreatment technologies[J]. Bioresour. Technol. 2009,100:4203-4213.
[129]Tsao G T, Ladish M R, Voloch M, et al. Production of ethanol and chemicals from cellulosic materials[J]. Process Biochem,1982,17:34-38
[130]Kumar P K Singh A, Schugerl K. Fed-batch culture for direct conversion of cellulosic substrates to acetic acid/ethanol Fusarium oxysporum[J].Proc Biochem,1991,26:209-216
[131]South C R, Hogsett D A L, Lynd L R. Modeling simultaneous saccharification and fermentation of lignocellulose to ethanol in batch and continuous reactors[J]. Enzyme and Microbial Technology,1995,17:797-803
[132]张继泉,王瑞明,关凤梅.玉米秸杆同时糖化发酵生产燃料酒精的研究明[J].纤维素科学与技术,2002,10(3)：35-39
[133][124]张德强,张志毅,黄镇亚.木质纤维生物量一步法((SSF)转化成乙醇的研究(Ⅲ)[J].北京林业大学学报,2000,22(6)：50-54
[134]Saddler J N. Bioconversion of forest and agricultural plant residues [M]. Oxford:CAB 1993:1-352
[135]Tantirungkij M, Nakashima N, Seki T, et al. Construction of xylose-assimilating cerevisiae[J].J Ferment Bioeng,1993,75:83-88
[136]Wilson DB:Cellulases. In Encyclopedia of Microbiology[M],3rd edn. Edited by Schaechter M. San Diego:Elsever Inc; 2009.
[137]Saha, B.C., Lignocellulose biodegradation and applications in biotechnology[M]. In: Saha, B.C., Hayashi, K. (Eds.), Lignocellulose Biodegradation. American Chemical Society, Washington, DC,2004
[138]Saha, B.C., Freer, S.N., Bothast, R.J., Production, purification, and properties of a thermostable beta-glucosidase from a color variant strain of Aureobasidium pullulans[J]. Appl. Environ. Microbiol.1994; 60,3774-3780.
[139]Haki, G.D., Rakshit, S.K. Developments in industrially important thermostable enzymes:areview[J]. Bioresour. Technol.2003; 89,17-34.
[140]Han, Y., Chen, H. Characterization of β-glucosidase from corn stover and its application in simultaneous saccharification and fermentation[J]. Bioresour. Technol.2008; 99,6081-6087.
[141]Shen, Y., Zhang, Y., Ma, T., Bao, X., Du, F., Qu, Y., Simultaneous saccharification and fermentation of acid-pretreated corncobs with a recombinant Saccharomyces cerevisiae expressing beta-glucosidase [J]. Bioresour. Technol.2007,99:5099-5103.
[142]Joglekar A V, Karanth N C; Srinivasan M C, Significance of (β-D-glucosidase in the measurement of exo-β-D-glucanase activity of cellulolytic fungi[J]. Enzyme and Microbial Technology.1983,5(1):25-29
[143]Ong, L.G., Abd-Aziz, S., Noraini, S., Karim, M.I., Hassan, M.A., Enzyme production and profile by Aspergillus niger during solid substrate fermentation using palm kernel cake as substrate[J]. Appl. Biochem. Biotechnol.2004; 118,73-79.
[144]Rie, K., Makoto, Y., Tomomi, T., Kiyohiko, I., Tsuyoshi, O., Hiromichi, N., Masahiro, S. Production and characterization of recombinant Phanerochaete chrysosporium β-glucosidase in the methylotrophic yeast pichia pastoris[J]. Biosci. Biotechnol. Biochem 2003; 67(1):1-7.
[145]Beguin, P., Aubert, J. P. The biological degradation of cellulose[J]. FEMS Microbiol. Rev 1994; 13:25-58.
[146]Siegel, D., Ira, M., Mara, D., Ben-Ami, B., Shouming, H., Stephen, G., Withers, Oded, S. Cloning, Expression, Characterization, and Nucleophile Identification of Family 3. Aspergillus niger β-Glucosidase[J], J. Boil. Chem 2000; 275(7):4973-4980.
[147]Daniel, J., Daroit, Silvana, T., Silveira, Plinho, F., Hertz, Adriano, B. Production of extracellular β-glucosidase by Monascus purpureus on different growth substrates[J]. Process Biochem 2007; 42:904-908.
[148]Maicas, S., Mateo, J.J. Hydrolysis of terpenyl glycosides in grape juice and other fruit juices:a review[J]. Appl. Microbiol. Biotechnol 2005; 67:322-335.
[149]Zheng Z., Shetty K. Solid-state bioconversion of phenolics from cranberry pomace and role of Lentinus edodes β-glucosidase[J]. J. Agric. Food. Chem 2000; 48:895-900.
[150]Saha, B.C., Freer, S.N., Bothast, R.J., Production, purification, and properties of a thermostable β-glucosidase from a color variant strain of Aureobasidium pullulans[J], Appl. Environ. Microbiol.1994,60:3774-3780.
[151]Haki, G.D., Rakshit, S.K. Developments in industrially important thermostable enzymes:a review[J]. Bioresour. Technol.2003,89:17-34.
[152]Han, Y., Chen, H. Characterization of β-glucosidase from corn stover and its application in simultaneous saccharification and fermentation[J]. Bioresour. Technol.2008, 99:6081-6087
[153]Shen, Y., Zhang, Y., Ma, T., Bao, X., Du, F., Qu, Y., Simultaneous saccharification and fermentation of acid-pretreated corncobs with a recombinant Saccharomyces cerevisiae expressing beta-glucosidase[J]. Bioresour. Technol.2007,99:5099-5103.
[154]Daniel, J., Daroit, Silvana, T., Silveira, Plinho, F., Hertz, Adriano, B. Production of extracellular β-glucosidase by Monascus purpureus on different growth substrates. Process Biochem 2007[J],42:904-908.
[155]Martins, L.F., Kolling, D., Camassola, M., Dillon, A.J.P., Ramos, L.P. Comparison of Penicillium echinulatum and Trichoderma reesei cellulases in relation to their activity against various cellulosic substrates[J], Bioresour. Technol.2008,99:1417-1424.
[156]Stemberg, D. β-Glucosidase of Trichoderma:Its Biosynthesis and Role in Saccharification of Cellulose[J], Appl. Environ. Microb.1976,31:648-654.
[157]欧阳嘉,李鑫,王向明,严明,徐琳.纤维素酶结合域的研究进展[M].生物加工过程.2008,6(2)：10-14
[158]Ilan Levy, Oded Shoseyov. Cellulose-binding domains, Biotechnological applications[J], Biotechnology Advances 2002,20:191-213
[159]郑小玲,林陈水.微生物纤维素结合域研究及其在生物技术中的应用[M].纤维素科学与技术,2008,16(2)：66-72
[160]Elena S. Lymar, Bin L., V. Renganathan. Purification and Characterization of a Cellulose-Binding P-Glucosidase from Cellulose-Degrading Cultures of Phanerochaete chrysosporium[J], Applied and Environmental Microbiology,1995(8):2976-2980
[161]Bin L., V. Renganathan. Gene Cloning and Characterization of a Novel Cellulose-Binding β-Glucosidase from Phanerochaete chrysosporium[J], Applied and Environmental Microbiology,1998(7):2748-2754
[162]Makoto Yoshida, Tsuyoshi Ohira, Kiyohiko Igarashi, et. al., Production and characterization of recombinant Phanerochaete chrysosporium cellobiose dehydrogenase in the methylotrophic yeast Pichia pastoris[J], bioscience biotechnology biochemistry.2001, 65(9):2050-2057
[163]Ria Kawai, Makoto Yoshida, Tomomi Tani, et.al, Production and characterization of recombinant Phanerochaete chrysosporium β-glucosidase in the methylotrophic yeast Pichia pastoris[J], bioscience biotechnology biochemistry.2003,67(1):1-7
[164]Diana Ciolacu, Janez Kovac, Vanja Kokol. The effect of the cellulose-binding domain from Clostridium cellulovorans on the supramolecular structure of cellulose fibers[J], Carbohydrate Research.2010(345):621-630
[165]Yu-San Liu, Yining Zeng, Yonghua Luo, Qi Xu, Michael E. Himmel,Steve J. Smith, Shi-You Ding, Does the cellulose-binding module move on the cellulose surface? Cellulose[J],2009,16:587-597
[166]Gao, J., Weng, H., Zhu, D., Yuan, M., Guan, F., Xi, Y. Production and characterization of cellulolytic enzymes from the thermoacidophilic fungal Aspergillus terreus Mll under solid-state cultivation of corn stover[J]. Bioresour. Technol 2008; 99:7623-7629.
[167]Hsieh, M.C., Graham, T.L. Partial purification and characterization of a soybean β-glucosidase with high specific activity towards isoflavone conjugates[J]. Phytochemistry 2001; 58:995-1005.
[168]Sue, M., Ishihara, A., Iwamura, H. Purification and characterization of a β-glucosidase from rye (Secale cereale L.) seedlings[J]. Plant Sci 2000; 155:67-74.
[169]Kim, J.S., Lee, Y.Y., Torget, R.W. Cellulose Hydrolysis under Extremely Low Sulfuric Acid and High-Temperature Conditions[J]. Appl. Biochem. Biothec 2001,91:331-340.
[170]Daniel, J., Daroit, Silvana, T., Silveira, Plinho, F., Hertz, Adriano, B. Production of extracellular β-glucosidase by Monascus purpureus on different growth substrates [J]. Process Biochem 2007; 42:904-908.
[171]Maicas, S., Mateo, J.J. Hydrolysis of terpenyl glycosides in grape juice and other fruit juices:a review[J]. Appl. Microbiol. Biotechnol 2005; 67:322-335.
[172]Zheng Z., Shetty K. Solid-state bioconversion of phenolics from cranberry pomace and role of Lentinus edodes (3-glucosidase[J]. J. Agric. Food. Chem 2000; 48:895-900.
[173]Paula Gonzalez Pombo, Gabriel Perez, Franciso Carrau, et. al., One-step purification and characterization of an intracellular β-glucosidase from Metschnikowia pulcherrima[J], Biotechnol. Lett.,2008,30:1469-1475
[174]Yejun Han, Hongzhang Chen, Characterization of β-glucosidase from corn stover and its application in simultaneous saccharification and fermentation[J], Bioresource Technology 2008,99:6081-6087
[175]Eduardo, B.M., Adriane, S.G., Ivone, C., Tetrahedron α-and P-glucosidase inhibitors: chemical structure and biological activiry[J], Tetrahedron 2006,62:10277-10302.
[176]Takano, M., Moriyama, R., and Ohmiya, K. Structure of a β-glucosidase gene from Ruminococcus albus and properties of the translated product[J]. J. Ferment. Bioeng.1992,73: 79-88.
[177]Pandey, M. and Mishra, S. Cloning and expression of P-glucosidase gene from the yeast Pichia etchellsii[J]. J. Ferment. Bioeng,1995,80:446-453.
[178]Magalhaes PO, Ferraz A, Milagres AF. Enzymatic properties of two β-glucosidases from Ceriporiopsis subvermispora produced in biopulping conditions[J]. J Appl Microbiol 2006,101:480-486.
[179]Kaur J, Bhupinder SC, Badhan AK, Ghatora, Kaur S. Purification and characterization of β-glucosidase from Melanocarpus spMTCC 3922[J]. Electron J Biotechnol 2007, 10:261-70.
[180]Valaskova V, Baldrian P. Degradation of cellulose and hemicelluloses by the brown rot fungus Piptoporus betulinus-production of extracellular enzymes and characterization of themajor cellulases[J]. Microbiology 2006,152:3613-3622.
[181]Lymar ES, Li B, Renganathan V. Purification and characterization of a cellulosebinding β-glucosidase from cellulose-degrading cultures of Phanerochaete chrysosporium[J]. Appl Environ Microbiol 1995,61:2976-80.
[182]Ozaki H, Yamada K, Isolation of streptomyces sp. Producing glucose-tolerant β-glucosidase and properities of the enzyme[J]. Agri. Biol. Chem.,1992,55:979-987
[183]Li X, Calza R E. Purification and characterization of extracellularβ-glucosidase from the rumen fungus Neocallimastix frontalis EB 188[J], Enzyme Microb Technol.,1991, 13:622-628
[184]Rie Kaiwai, Makoto Yoshida, Tomomi Tani, et. al, Production and characterization of recombinant Phanerochaete chrysosporium β-Glucosidase in the Methylotrophic Yeast Pichia pastoris[J], Biosci. Biotechnol. Biochem.,2003,67(1):1-7
[185]Vasanti Deshpande, Karl-Erik Eriksson, and Bert Pettersson, Production, Purification and Partial Characterization of 1,4-β-glucosidase Enzymes from Sporotrichum pulverulentum[J], Eur. J. Biochem.1978,90:191-198
[186]Elena S. Lymar, Bin L, V. Renganathan, Purification and Characterization of a Cellulose-Binding P-Glucosidase from Cellulose-Degrading Cultures of Phanerochaete chrysosporium[J], Applied and Environment Microbiology,1995,61(8):2976-2980
[187]Ghose T K. Measurement of cellulase activities[J]. Pure Appl Chem,1987,59 (2): 257-268.
[188]Claeyssens, M., Aerts, G., Characterization of cellulolytic activities in commercial Trichoderma reesei preparations:an approach using small, chromogenic substrates[J]. Bioresour. Technol.1992,39,143-146.
[189]Ghose, T.K., Measurement of cellulase activities[J]. Pure Appl. Chem.1986,59, 257-268.
[190]Bailey, M.J., Biely, P., Poutanen, K., Interlaboratory testing of methods for assay of xylanase activity[J]. J. Biotechnol.1992,23:257-270.
[191]彭汀汀,董宏平,彭惠等,一株具木聚糖酶活链霉菌的鉴定及其木聚糖降解酶系分析[M],南京师大学报(自然科学版),2006,29(4)：73-78
[192]Duff, S. J. B. and W. D. Murray. Bioconversion of forest products industry waste cellulosics to fuel ethanol:Areview[J]. Bioresource Technology 1996,55:1-33.
[193]Marimuthu Jeya, Ye-Wang Zhang, In-Won Kim, et, al. Enhanced saccharification of alkali-treated rice straw by cellulase from Trametes hirsuta and statistical optimization of hydrolysis conditions by RSM[J]., Bioresource Technology 2009 (100):5155-5161
[194]Chen, H., Liu, L., Unpolluted fractionation of wheat straw by steam explosion and ethanol extraction[J]. Bioresour. Technol.2007,98,666-676.
[195]Chang VS, Burr B, Holtzapple MT. Lime pretreatment of switchgrass[J]. Appl. Biochem. Biotechnol.1997,63(65):3-19.
[196]Chang VS, Nagwani M, Holtzapple MT. Lime pretreatment of crop residues:bagasse and wheat straw[J]. Appl. Biochem. Biotechnol.1998,74:135-159.
[197]刘书钗.制浆造纸分析与检测[M].化学工业出版社,2003：17-31.
[198]Agu, R.C., Amadife, A.E., Ude, C.M., Onyia, A., Ogu, E.O., Okafor, M., Ezejiofor, E., 1997. Combined heat treatment and acid hydrolysis of cassava grate waste (CGW) biomass for ethanol production[M]. Waste Manage. (Oxford) 17,91-96.
[199]Liu, S.C., Analysis and Measurement in Papermaking Industry[M]. Chemical Industry Press, Beijing.2004:19-27.
[200]S. Hari Krishna, K. Prasanthi, G. V. Chowdary and C. Ayyanna, Simultaneous saccharification and fermentation of pretreated sugar cane leaves to ethanol[J], Process Biochemistry,1998,33(8):825-830,
[201]Yejun Han, Hongzhang Chen, Characterization of b-glucosidase from corn stover and its application in simultaneous saccharification and fermentation[J], Bioresource Technology 2008(99):6081-6087
[202]Takagi, M., Abe, S., Suzuki, S., Emert, G. H. and Yara, N., A method for production of alcohol directly from cellulose using cellulase and yeast. In Proceedings of Bioeonversion of Celhdosie Substances into Energy[J], Chemicals and Microbial Protein, ed. T. K. Ghose. J.I.T., Delhi,1977.551-571.
[203]Krishna, S.H., Reddy, T.J., Chowdary, G.V., Simultaneous saccharification and fermentation of lignocellulosic wastes to ethanol using a thermotolerant yeast[J], Bioresour. Technol.2001,77:193-196.
[204]Shen, Y., Zhang, Y., Ma, T., Bao, X., Du, F., Qu, Y., Simultaneous saccharification and fermentation of acid-pretreated corncobs with a recombinant Saccharomyces cerevisiae expressing beta-glucosidase[J]. Bioresour. Technol.2007,99:5099-5103.
[205]Sue, M., Ishihara, A., Iwamura, H., Purification and characterization of a b-glucosidase from rye (Secale cereale L.) seedlings[J]. Plant Sci.2000,155:67-74.
[206]Xiao, Z., Zhang, X., Gregg, D., Saddler, J.N., Effects of sugar inhibition on cellulases and b-glucosidase during enzymatic hydrolysis of softwood substrates[J]. Appl. Biochem. Biotechnol.2004,115:1115-1126.
[207]Chen, M., Zhao, J., Xia, L., Enzymatic hydrolysis of maize straw polysaccharides for the production of reducing sugars[J]. Carbohyd. Polym.2008,71:411-415
[208]Saha, B.C., Cotta, M.A., Lime pretreatment, enzymatic saccharification and fermentation of rice hulls to ethanol[J]. Biomass Bioenergy 2008,32:971-977.
[209]Adsul, M.G, Bastawde, K.B., Varma, A.J., Gokhale, D.V., Strain improvement of Penicillium janthinellum NCIM 1171 for increased cellulase production[J]. Bioresour. Technol.2007,98:1467-1473.
[210]Zhang, Q., Cai, W., Enzymatic hydrolysis of alkali-pretreated rice straw by Trichoderma reesei ZM4-F3[J], Biomass Bioenergy 2008,32:1130-1135.
[211]Saha, B.C., Iten, L.B., Cotta, M.A., Wu, Y.V., Dilute acid pretreatment, enzymatic saccharification and fermentation of wheat straw to ethanol[J]. Process Biochem.2005,40: 3693-3700.
[212]Kaar, W.E., Gutierrez, C.V., Kinoshita. C.M., Steam explosion of sugarcane bagasse as a pretreatment for conversion to ethanol[J]. Biomass Bioenergy.1998,14:277-287.
[213]Vlasenko, E.Y., Ding, H., Labavitch, J.M., Shoemaker, S.P., Enzymatic hydrolysis of pretreated rice straw[J]. Bioresour. Technol.1997,59:109-119.
[214]Marimuthu Jeya, Ye-Wang Zhang, In-Won Kim, Jung-Kul Lee. Enhanced saccharification of alkali-treated rice straw by cellulase from Trametes hirsuta and statistical optimization of hydrolysis conditions by RSM[J], Bioresource Technology 2009,100: 5155-5161
[2]Kim S, Dale B E. Global potential bioethanol production from wasted crops and crop residues[J]. Biomass and Bioenergy,2004,26:361-375
[3]Hill, J., Nelson, E., Tilman, D., Polasky, S.& Tiffany, D. Environmental, economic, and energetic costs and benefits of biodiesel and ethanol biofuels[M]. Proc. Natl Acad. Sci. USA 2006,103:11206-11210
[4]Kubicek, C.P., Messner, R., Gruber, F., Mach, R.L., and Kubicek-Pranz, E.M.1993. The Trichoderma cellulase regulatory puzzle:from the interior life of a secretory fungus[J]. Enz. Microb. Technol.15:90-99.
[5]Rosi, I., Vinella, M., and Domezio, M.1994. Characterization of β-glucosidase activity in yeasts of enological origin[J]. J. Appl. Bact.77:519-527.
[6]Esen, A. β-glucosidases:overview, in β-Glucosidases:Biochemistry and Molecular Biology[M], Esen, A., Ed., American Chemical Society, Washington, DC,1993:1-14.
[7]Fredrickson, D.S., and Sloan, H.R. The Metabolic Basis of Inherited Disease[M]. (Stanbury, J.B., Wygnaarden, J.B., and Fredrickson, D.S., Eds.) McGraw-Hill, New York,1972:7730.
[8]Henrissat, B. A classification of glycosyl-hydrolases based on amino acid sequence similarities[J]. Biochem. J.1991,293:781-788.
[9]Henrissat, B. and Bairoch, A. Updating the sequence-based classification of glycosyl hydrolases[J]. Biochem. J.1996,316:695-696.
[10]Cantarel BL, Coutinho PM, Rancurel C, Bernard T, Lombard V, Henrissat B. The Carbohydrate-Active EnZymes database (CAZy):an expert resource for glycogenomics[J]. Nucleic Acids Res 2009,37:233-238
[11]Henrissat B. A classification of glycosyl hydrolases based on amino acid sequence similarities[J]. Biochem J 1991,280:309-316
[12]Opassiri R, Pomthong B, Akiyama T, Nakphaichit M, Onkoksoong T, Ketudat-Cairns M, Ketudat Cairns JR A stress-induced rice b-glucosidase represents a new subfamily of glycosyl hydrolase family 5 containing a fascin-like domain[J]. Biochem J 2007,408:241-249
[13]Wohler F., Liebig J. Annu. Pharm.1837,22:1-24
[14]Ander F, Lars R. Expression of azeatin-glucoside-degrading β-glucosidase in Brassicanapus. Plant-Physiolgy(USA) [J],1995,108:1369-1377
[15]Barrett T, Suresh C G. Tolley S P, Dodson E J, Hughes M A. The crystal structure of a cyanogenic B-glucosidase from white clover, a family 1 glycosyl hydrolase[J]. Structure. 1995,3:951-960
[16]Yukti Bhatia, Saroj Mishra, and V.S. Bisaria, Microbial β-Glucosidases:Cloning, Properties, and Applications[J]. Critical Reviews in Biotechnology,2002.22(4):375-407
[17]Sternberg D. (3-Glucosidase of Trichoderma:its biosynthesis and role in saccharification ofcellulose[J].Applied and Environmental Microbiology,1976,31(5):648-654
[18]Awafo V A, Chahal D S, Simpson B K. Evaluation of combination treatments of sodium xyoxide steam explosion for the production of cellulose-systems by two Trichoderma mutants underand solid-state fermentation conditions[J]. Bioresource technology,2000,73(3): 235-245
[19]Tangnu S K, Blanch H W, Wilke C R. Enhanced production of cellulase, hemicellulase and β-glucosidase by Trichoderma reesei[J]. Biotech Bioengin,1981,23,1837-1849
[20]Jianmin Gao, Haibo Weng, Daheng Zhu, Mingxue Yuan, Fangxia Guan, Yu Xi, Production and characterization of cellulolytic enzymes from the thermoacidophilic fungal Aspergillus terreus M11 under solid-state cultivation of corn stover[J]. Bioresource Technology 2008,99: 7623-7629
[21]杨建海,任大明.黑曲霉p-葡萄糖苷酶高产菌株的Co60-52-23的选育[J]，食品与发酵工业,2005，31(6)：147-150
[22]Hida, H., Yamada, T., Yamada, Y., Genome shuffling of Streptomyces sp. U121 for improved production of hydroxycitric acid[J]. Appl. Microbiol. Biotechnol.2007,73: 1387-1393.
[23]Lin, J., Shi, B.H., Shi, Q.Q., He, Y.X., Wang, M.Z.. Rapid improvement in lipase production of Penicillium expansum by genome shuffling[J]. Chin. J. Biotechnol.2007,23:672-676.
[24]Yao, Q., Sun, T.T., Liu, W.F., Chen, G.J., Gene cloning and heterologous expression of a novel endoglucanase, swollenin, from Trichoderma pseudokoningii S38[J]. Biosci. Biotechnol. Biochem.2008,72:2799-2805.
[25]Fengchao Wang, Fan Li, Guanjun Chen, Weifeng Liiu. Isolation and characterization of novel cellulase genes from uncultured microorganisms in different environmental niches[J], Microbiological Research,2009,164(6):650-657.
[26]Philip Hugenholtz and Gene W. Tyson, Metagenomics, nature,2008,455(25),481-483
[27]Susannah Green Tringe and Edward M. Rubin, Metagenomics DNA sequencing of environmental samples[J], nature reviews genetics,2005,6:805-814
[28]Nathan Blow. Exploring unseen communities, Technology feature metagenomics[J], nature, 2008,453(29):687-690
[29]E. Kalogeris, P. Christakopoulos, P. Katapodis, A. Alexiou, S. Vlachou, D. Kekos, B.J. Macris Production and characterization of cellulolytic enzymes from the thermophilic fungus Thermoascus aurantiacus under solid state cultivation of agricultural wastes[J]. Process Biochemistry,2003,38:1099-1104
[30]Yejun Han, Hongzhang Chen, Characterization of beta-glucosidase from corn stover and its application in simultaneous saccharification and fermentation[J], Bioresource Technology 2008,99:6081-6087
[31]Butters TD. Gaucher disease[M]. Curr Opin Chem Biol 2007,11:412-418
[32]Dvir H, Harel M, McCarthy AA, Toker L, Silman I, Futerman AH, Sussman JLX-ray structure of human acid-β-glucosidase, the defective enzyme in Gaucher disease[J]. EMBO Rep 2003,4:704-709
[33]Lieberman RL, Wustman BA, Huertas P, Powe AC, Pine CW, Khanna R, Schlossmacher MG, Ringe D, Petsko GAStructure of acid β-glucosidase with pharmacological chaperone provides insight into Gaucher disease[J]. Nat Chem Biol 2007,3:101-107
[34]Matern H, Boermans H, Lottspeich F, Matern S Molecular cloning and expression of human bile acid beta-glucosidase. J Biol Chem 2001,276:37929-37933
[35]Yildiz Y, Matern H, Thompson B, Allegood JC, Warren RL, Ramirez DMO, Hammer RE, Hamra FK, Matern S, Russell DW beta-Glucosidases Mutation of b-glucosidase 2 causes glycolipid storage disease and impaired male fertiliry[J]. J Clin Invest 2006,116:2985-2994
[36]Boot RG, Verhoek M, Donker-Koopman W, Strijland A, van Marie J, Overkleeft HS, Wennekes T, Aerts JM Identification of the non-lysosomal glucosylceramidase as betaglucosidase 2[J]. J Biol Chem 2007,282:1305-1312
[37]Hayashi Y, Okino N, Kakuta Y, Shikanai T, Tani M, Narimatsu H, Ito M Klotho-related protein is a novel cytosolic neutral β-glycosylceramidase[J]. J Biol Chem 2007,282: 30889-30900
[38]Day AJ, DuPont MS, Ridley S, Rhodes M, Rhodes MJ, Morgan MR, Williamson G Deglycosylation of flavonoid and isoflavonoid glycosides by human small intestine and liver β-glucosidase activity[J]. FEBS Lett 1998,436:71-75
[39]Berrin J-G, McLauchlan WR, Needs P, Williamson G, Puigserver A, Kroon PA, Juge N Functional expression of human liver cytosolic β-glucosidase in Pichia pastoris. Insights into its role in the metabolism of dietary glucosides[J]. Eur J Biochem 2002,269:249-258
[40]Zagrobelny M, Bak S, M(?)ller BL Cyanogenesis in plants and arthropods [J]. Phytochemistry 2008,69:1457-1468
[41]Ferrieira AHP, Marana SR, Terra WR, Ferreira C Purification, molecular cloning, and properties of a b-glycosidase isolated from midgut lumen of Tenebrio molitor (Coleoptera) larvae[J]. Insect Biochem Mol Biol 2001,31:1065-1076
[42]Jones AME, Bridges M, Bones AM, Cole R, Rossiter JT Purification and characterisation of a non-plant myrosinase from the cabbage aphid Brevicoryne brassicae[J]. Insect Biochem Mol Biol 2001,31:1-5
[43]Marana SR, Jacobs-Lorena M, Terra WR, Ferrieira C Amino acid residues involved in substrate binding and catalysis in an insect digestive β-glycosidase[J]. Biochim Biophys Acta 2001,1545:41-52
[44]Malboobi MA. Lefebvre D. A phosphate-starvation inducible β-glucosidase gene (psr3.2) isolated from Arabidopsis thaliana is a member of a distinct subfamily of the BGA family[J]. Plant Mol Biol 1997,34:57-68
[45]van de Ven WT, LeVesque CS, Perring TM, Walling LL Local and systemic changes in squash gene expression in response to silver winged whitefly feeding[J]. Plant Cell 2000, 12:1409-1423
[46]Xu Z, Escamilla-Trevino LL, Zeng L, Lalgondar M, Bevan DR, Winkel BSJ, Mohamed A, Cheng C, Shih M, Poulton JE, Esen A Functional genomic analysis of Arabidopsis thaliana glycoside hydrolase family 1[J]. Plant Mol Biol 2004,55:343-367
[47]Opassiri R, Pomthong B, Okoksoong T, Akiyama T, Esen A, Ketudat Cairns JR Analysis of rice glycosyl hydrolase family 1 and expression of Os4bglul2 β-glucosidase[J]. BMC Plant Biol 2006,6:33
[48]Thorlby G, Fourier N, Warren G. The SENSITIVE TO FREEZING2 gene, required for freezing tolerance in Arabidopsis thaliana, encodes a beta-glucosidase[J]. Plant Cell 2004, 16:2192-2203
[49]Marques AR, Coutinho PM, Videira P, Fialho AM, S-Correia I Sphingomonas paucimobilis beta-glucosidase Bgll:a member of a new bacterial subfamily in glycoside hydrolase family 1[J]. Biochem J 2003,370:793-804
[50]Niemeyer HM Hydroxamic acids (4-hydroxy-l,4-benzoxazin-3-ones), defense chemicals in the Gramineae[J]. Phytochemistry 1988,27:3349-3358
[51]Poulton JE Cyanogenesis in plants[J]. Plant Physiol 1990,94:401-405
[52]Morant AV, J(?)gensen K, Jorgensen C, Paquette SM, Sa'nche'z-Perez R, Moller BL, Bak S b-Glucosidases as detonators of plant chemical defense[J]. Phytochemistry 2008, 69:1795-1813
[53]Sherameti I, Venus Y, Drzewiecki C, Tripathi W, Dan VM, Nitz I, Varma A, Grundler F, Oelmu"ller R PYK10, a b-glucosidase located in the endoplasmatic reticulum, is crucial for the beneficial interaction between Arabidopsis thanliana and the endophytic fungus Piriformospora indica[J]. Plant J 2008,54:428-439
[54]Hrmova M, Harvey AJ, Wang J, Shirley NJ, Jones GP, Stone BA, Hoj PB, Fincher GB Barley beta-D-glucan exohydrolases with β-D-glucosidase activity[J]. J Biol Chem 1996, 271:5277-5286
[55]Hrmova M, MacGregor EA, Biely P, Stewart RJ, Fincher GB Substrate binding and catalytic mechanism of a barleyβ-D-glucosidase/(1,4)-β--D-glucan exohydrolase[J]. J Biol Chem 1998,273:11134-11143
[56]Hrmova M, Burton RA, Biely P, Lahnstein J, Fincher GB Hydrolysis of (1,4)-β-D-mannans in barley (Hordeum vulgare L.) is mediated by the concerted action of (1,4)-β-D-mannan endohydrolase and β-D-mannosidase[J]. Biochem J 2006,399:77-90
[57]Akiyama T, Kaku H, Shibuya N. A cell wall-bound b-glucosidase from germinated rice: purification and properties[J]. Phytochemistry 1998,48:49-54
[58]Opassiri R, Ketudat Cairns JR, Akiyama T, Wara-Aswapati O, Svasti J, Esen A Characterization of a rice b-glucosidase highly expressed in flower and germinating shoot[J]. Plant Sci 2003,165:627-638
[59]Opassiri R, Hua Y, Wara-Aswapati O, Akiyama T, Svasti J, Esen A, Ketudat Cairns JR beta-Glucosidase, exo-beta-glucanase and pyridoxine transglucosylase activities of rice BGlul[J]. Biochem J 2004,379:125-131
[60]Seshadri S, Akiyama T, Opassiri R, Kuaprasert B, Ketudat Cairns J Structural and enzymatic characterization ofOs3BGlu6, a rice b-glucosidase hydrolyzing hydrophobic glycosides and (1-3)-and (1-2)-linked disaccharides[J]. Plant Physiol 2009,151:47-58
[61]Hosel W, Surholt E, Borgmann E Characterization of b-glucosidase isoenzymes possibly involved in lignification from chick pea (Cicer arietinum L.) cell suspension culture[J]. Eur J Biochem 1978,84:487-492
[62]Schliemann W Hydrolysis of conjugated gibberellins by beta-glucosidases from dwarf rice (Oryza sativa L. cv. Tan-ginbozu) [J]. J Plant Physiol 1984,116:123-132
[63]Brzobohaty'B, Moore I, Kristoffersen P, Bako L, Campos N, Schell J, Palme K Release of active cytokinin by a β-glucosidase localized to the maize root meristem[J]. Science 1993, 262:1051-1054
[64]Dietz K-J, Sauter A, Wichert K, Messdaghi D, Hartung W Extracellular b-glucosidase activity in barley involved in the hydrolysis of ABA glucose conjugate in leaves[J]. J Exp Bot 2000,51:937-944
[65]Jakubowska A, Kawalczyk S A specific enzyme hydrolyzing 6-0(4-0)-indole-3-ylacetyl-β-D-glucose in immature kernels of Zea mays[J]. J Plant Physiol 2005,162:207-213
[66]Crout DH, Vic G Glycosidases and glycosynthetases in intermediate in the biosynthesis of monoterpenoid indole alka-glycoside and oligosaccharide synthesis[J]. Curr Opin Chem Biol loids. J Chem Soc Chem Commun 1998:98-111
[67]Barleben L, Panjikar S, Ruppert M, Koepke J, Sto'ckigt J Henrissat B, Callebaut I, Fabrega S, Lehn P, Mornon JP, Davies Molecular architecture of strictosidine glucosidase:the gateway G Conserved catalytic machinery and the prediction of a to the biosynthesis of the monoterpenoid indole alkaloid family. Common fold for several families of glycosyl hydrolases. Proc Plant Cell 19:2886-2897 Natl Acad Sci USA 92:7090-7094
[68]Jenkins J, Lo Leggio L, Harris G, Pickersgill R., Beta-Molecular cloning and functional bacterial expression of a plant glucosidase, beta-galactosidase, family A cellulases, family F β-glucosidase specifically involved in alkaloid biosynthesis. xylanases and two barley glycanases form a superfamily of Phytochemistry[M].1995,54:657-666
[69]Nomura T, Quesada AL, Kutchan TM. The new beta-D-glucosidase in terpenoid isoquinoline alkaloid biosynthesis in Psychotria ipecacuanha[J]. J Biol Chem 2008, 283:34650-34659
[70]Reuveni M, Sagi Z, Evnor D, Hetzroni A b-Glucosidase activity is involved in scent production in Narcissus flowers[J]. Plant Sci 1999,147:19-24
[71]Mattiacci L, Dicke M, Posthumus MA Beta-glucosidase:an elicitor of herbivore-induced plant odor that attracts host-searching parasitic wasps[J]. Proc Natl Acad Sci USA 1995, 92:2036-2040
[72]Gilbert HJ, Brumer H How the walls come tumbling down:recent structural biochemistry of plant poly-saccharide degradation[J]. Curr Opin Plant Biol 2008,11:338-348
[73]Doi RH, Kosugi A Cellulosomes:plant-cell-wall-degrading enzyme complexes[J]. Nat Rev Microbiol 2004,2:541-551
[74]Carvalho AL, Dias FM, Nagy T, Prates JA, Proctor MR, Smith N, Bayer EA, Davies GJ, Ferreira LM, Roman?oMJ, Fontes CM, Gilbert HJ., Evidence for a dual binding mode of dockerin modules to cohesins[J]. Proc Natl Acad Sci USA 2007(104):3089-3094
[75]Lymar ES, Li B, Renganathan V. Purification and characterization of a cellulose-binding β-glucosidase from cellulose degrading cultures of Phanerochaete chrysosporium[J]. Appl Environ Microbiol 1995,61:2976-2980
[76]Igarashi K, Tani T, Kawal R, Samejima M Family 3 b-glucosidase from cellulose-degrading culture of the white-rot fungus Phanerochaete chrysosporium[J], J Biosci Bioeng 2003, 95:572-576
[77]Henrissat B, Callebaut I, Fabrega S, Lehn P, Mornon JP, Davies G Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases[J]. Proc Natl Acad Sci USA 1995,92:7090-7094
[78]Jenkins J, Lo Leggio L, Harris G, Pickersgill R Beta-glucosidase, beta-galactosidase, family A cellulases, family F xylanases and two barley glycanases form a superfamily of enzymes with 8-fold beta/alpha architecture and with two conserved glutamates near the carboxy-terminal ends of beta strands four and seven[J]. FEBS Lett 1995,362:281-285
[79]Sanz-Aparicio J, Hermoso JA, Martinez-Ripoll M, Lequerica JL, Polaina J Crystal structure of beta-glucosidase A from Bacillus polymyxa:insights into the catalytic activity in family 1 glycosyl hydrolases[J]. J Mol Biol 1998,275:491-502
[80]Varghese J N, Hrmova M, FincherGBThree-dimensional structure of a barley β-D-glucan exohydrolase; a family 3 glycosyl hydrolase[J]. Structure 1999,7:179-190
[81]Hrmova M, Varghese JN, De Gori R, Smith BJ, Driguez H, Fincher GB Catalytic mechanisms and reaction intermediates along the hydrolytic pathway of a plant β-D-glucan glucohydrolase[J]. Structure 2001,9:1005-1016
[82]Park JK, Wang L-X, Patel HV, Roseman S Molecular cloning and characterization of a unique β-glucosidase from Vibrio cholorae[J]. J Biol Chem 2002,277:29555-29560
[83]Qi M, Jun H-S,Forsbert CW., Ce19D,anatypical 1,4-β-D-glucan glucohydrolase from Fibrobacter succinogenes:characteristics, catalytic residues, and synergistic interactions with other cellulases[J]. J Bacteriol 2008,109:1976-1984
[84]Gracia Gonza'lez-Blasco, Juliana Sanz-Aparicio§, Beatriz Gonza'lez, Juan A. Hermoso, Julio Polaina, Directed Evolution of beta-Glucosidase A from Paenibacillus polymyxa to Thermal Resistance[J], The Jouranl of Biological Chemistry 2000,18(5):13708-13712
[85]Davies GJ, Ducros VM-A, Varrot A, Zechel DL Mapping the conformational itinerary of beta-glucosidases by X-ray crystallography [J]. Biochem Soc Trans 2003,31:523-527
[86]Czjzek M, Cicek M, Zamboni V, Bevan DR, Henrissat B, Esen A The mechanism of substrate (aglycone) specificity in b-glucosidases is revealed by crystal structures of mutant maize β-glucosidase-DIMBOA,-DIMBOAGlc, and dhurrin complexes[J]. Proc Natl Acad Sci USA 2000,97:13555-13560
[87]Bauer M W, Kelly R M. The family β--glucosidases from Pyrococcus furiosus and Agrobacterium faecalis share a common catalytic mechanism[J]. Biochemistry,1998,37: 17170-17178
[88]Zechel DL, Boraston AB, Gloster TM, Boraston CM, Macdonald JM, Tilbrook DMG, Stick RV, Davies GJ Iminosugar glycosidase inhibitors:structural and thermodynamic dissection of the binding of isofagomine and 1-deoxynojirimycin to β-glucosidases[J]. J Am Chem Soc 2003,125:14313-14323
[89]Vincent F, Gloster TM, Macdonald J, Morland C, Stick RV, Dias FM, Prates JA, Fontes CM, Gilbert HJ, Davies GJ Common inhibition of both beta-glucosidases and betamannosidases by isofagomine lactam reflects different hydrolysis [J]. Chembiochem 2004,5:1596-1599
[90]Gloster TM, Macdonald JM, Tarling CA, Stick RV, Withers SG, Davies GJ Structural, thermodynamic, and kinetic analyses of tetrahydroozazine-derived inhibitors bound to beta-glucosidases[J]. J Biol Chem 2004,279:29236-49242
[91]Ly HD, Withers SG Mutagenesis of glycosidases. Annu Rev Biochem 1999,68:487-522
[92]Marana SR Molecular basis of substrate specificity in family 1 glycoside hydrolases[J]. IUBMB Life 2006,58:63-73
[93]Verdoucq L, Czjzek M, Moriniere J, Bevan DR. Esen A Mutational and structural analysis of aglycone specificity in maize and sorghum beta-glucosidases[J]. J Biol Chem 2003, 278:25055-25062
[94]Berrin J-G, Czjzek M, Kroon PA, McLauchlan WR, Puigserver A, Williamson G. Juge N Substrate (aglycone) specificity of human cytosolic bete-glucosidase[J]. Biochem J 2003, 373:41-48
[95]Cicek M, Blanchard D, Bevan DR, Esen A The aglycone specificity-determining sites are different in 2,4-dihydroxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA)-glucosidase (maize beta-glucosidase) and dhurrinase (sorghum beta-glucosidase) [J]. J Biol Chem 2000,275: 20002-20011
[96]刘望夷,祁国荣.真核生物核糖体RNA基因的结构与表达[M].北京：科学出版社,1989：46-94
[97]Srisomsap C, Svasti J, Surarit R, Champattanachai V, Sawangareetrakul P, Boonpuan K, Subhasitanont P, Chokchaichamnankit D Isolation and characterization of an enzyme with beta-glucosidase and beta-fucosidase activities from Dalbergia cochinchinensis Pierre[J]. J Biochem 1996,119:585-590
[98]Gloster TM, Meloncelli P, Stick RV, Zechel D, Vasella A, Davies GJ Glycosidase inhibition: an assessment of the binding of 18 putative transition-state mimics[J]. J Am Chem Soc 2007, 129:2345-2354
[99]Zollner H., Handbook of enzyme inhibitors[M]. VCH, Weinheim,1989:94-95
[100]Burmeister WP, Cottaz S, Rollin P, Vasella A, Henrissat B High resolution X-ray crystallography shows that ascorbate is a cofactor for myrosinase and substitutes for the function of the catalytic base[J]. J Biol Chem 2000,275:39385-39393
[101]Nam KH. Kim S-J, Kim M-Y, Kim JH, Yeo Y-S, Lee C-M, Jun H-K, Hwang KY Crystal structure of engineered beta-glucosidase from soil metagenome[J]. Proteins 2008, 73:788-793
[102]Chi YI, Martinez-Cruz LA, Jancarik J, Swanson RV, Robertson DE, Kim SH Crystal structure of the beta-glycosidase from the hyperthermophile Thermosphaera aggregans: insights into its activity and thermostability[J]. FEBS Lett 1999,445:375-383
[103]Yin, J., Liu, D., Strategic thinking on developing petroleum substitutes in China[J]. Petroleum Sci.2006,3:46-51.
[104]Rass-Hansen, J., Falsig, H., Jorgensen, B., Christensen, C.H., Bioethanol:fuel or feedstock? [J], J. Chem. Technol. Biotechnol.2007,82:329-333.
[105]Qu, Y.B., Zhu, M.T., Liu, K., Bao, X.M., Lin, J.Q., Studies on cellulosic ethanol production for sustainable supply of liquid fuel in China[J]. Biotechnol. J.2006,1: 1235-1240
[106]Sanchez, J., Jiang, J.,2008. China, People's Republic of:Bio-fuels annual 2008[J]. USDA, FAS. Gain Report Number CH8052.
[107]Li, S.Z., Chan-Halbrendt, C., Ethanol production in China:potential and technologies[J]. Appl. Energy 2009,4:4-9.
[108]Yang, B., Lu, Y., The promise of cellulosic ethanol production in China[J]. J. Chem. Technol. Biotechnol.2007,82:6-10.
[109]Qu, Y.B., Zhu, M.T., Liu, K., Bao, X.M., Lin, J.Q., Studies on cellulosic ethanol production for sustainable supply of liquid fuel in China[J]. Biotechnol. J.2006,1:1235-1240
[110]Zhang, S.P., Yan, Y.J., Ren, Z.W., Li, T.C., Fuel ethanol production from lignocellulosic biomass[J]. Prog. Chem. (Chinese) 2007,19:1129-1133.
[111]Yao, R.S., Qi, B.K., Deng, S.S., Liu, N., Peng, S.C., Cui, Q.F., Use of surfactants in enzymatic hydrolysis of rice straw and lactic acid production from rice straw by simultaneous saccharification and fermentation[J]. Bioresour.2007,2:389-398.
[112]Shen, Y., Zhang, Y., Ma, T., Bao, X.M., Du, F.G., Zhuang, G.Q., Qu, Y.B., Simultaneous saccharification and fermentation of acid-pretreated corncobs with a recombinant Saccharomyces cerevisiae expressing beta-glucosidase[J]. Bioresour. Technol.2008,99: 5099-5103.
[113]Wyman, C.E., What is (and is not) vital to advancing cellulosic ethanol[J]. Trends Biotechnol.2007,25:153-157.
[114]Gruno, M., Valjamae, P., Pettersson, G., Johansson, G., Inhibition of the Trichoderma reesei cellulases by cellobiose is strongly dependent on the nature of the substrate[J]. Biotechnol. Bioeng.2004,86:503-511
[115]Hou, J., Shen, Y., Li, X.P., Bao, X.M., Effect of the reversal of coenzyme specificity by expression of mutated Pichia stipitis xylitol dehydrogenase in recombinant Saccharomyces cerevisiae[J]. Lett. Appl. Microbiol.2007,45:184-189.
[116]Galbe, M., Zacchi, G., Pretreatment of lignocellulosic materials for efficient bioethanol production[J]. Adv. Biochem. Eng. Biotechnol.2007,108:41-65.
[117]Sanchez, C., Lignocellulosic residues:biodegradation and bioconversion by fungi[J]. Biotechnol. Adv.2009,27:185-194.
[118]Ma, H., Liu, W.W., Chen, X., Wu, Y.J., Yu, Z.L., Enhanced enzymatic saccharification of rice straw by microwave pretreatment[J]. Bioresour. Technol.2009,100:1279-1284.
[119]Chen, H., Han, Y., Xu, J., Simultaneous saccharification and fermentation of steam exploded wheat straw pretreated with alkaline peroxide[J]. Process Biochem.2008,43: 1462-1466.
[120]Cheng, K., Cai, B., Zhang, J., Ling, H., Zhou, Y., Ge, J., Xu, J., Sugarcane bagasse hemicellulose hydrolysate for ethanol production by acid recovery process[J]. Biochem. Eng. J.2008,38:105-109.
[121]Li, L., Li, X.Z., Tang, W.Z., Zhao, J., Qu, Y.B., Screening of a fungus capable of powerful and selective delignification on wheat straw[J]. Lett. Appl. Microbiol.2008,47: 415-420.
[122]Sun, Y., Cheng, J., Hydrolysis of lignocellulosic materials for ethanol production:a review[J]. Bioresour. Technol.2002,83:1-11.
[123]Jing, X.Y., Zhang, X.X., Bao, J., Inhibition performance of lignocellulose degradation products on industrial cellulase enzymes during cellulose hydrolysis[J]. Appl. Biochem. Biotechnol.2009,87:34-40.
[124]Liu, K., Lin, X., Yue, J., Li, X., Fang, X., Zhu, M., Lin, J., Qu, Y., Xiao, L., High concentration ethanol production from corncob residues by fed-batch strategy[J]. Bioresour. Technol.,2009,83:81-87.
[125]Zhao, X., Cheng, K., Liu, D., Organosolv pretreatment of lignocellulosic biomass for enzymatic hydrolysis[J]. Appl. Microbiol. Biotechnol.2009,82:815-827.
[126]Zhu, S.D., Wu, Y.X., Yu, Z.N., Liao, J.T., Zhang, Y., Pretreatment by microwave/alkali of rice straw and its enzymic hydrolysis[J]. Process Biochem.2005,40:3082-3086.
[127]Zeng, W., Chen, H., Synergistic effect of feruloyl esterase and cellulase in hydrolyzation of steam-exploded rice straw[J]. Chin. J. Biotechnol.2009,25:49-54
[128]Kumar, R., Wyman, C.E., Effect of xylanase supplementation of cellulase on digestion of corn stover solids prepared by leading pretreatment technologies[J]. Bioresour. Technol. 2009,100:4203-4213.
[129]Tsao G T, Ladish M R, Voloch M, et al. Production of ethanol and chemicals from cellulosic materials[J]. Process Biochem,1982,17:34-38
[130]Kumar P K Singh A, Schugerl K. Fed-batch culture for direct conversion of cellulosic substrates to acetic acid/ethanol Fusarium oxysporum[J].Proc Biochem,1991,26:209-216
[131]South C R, Hogsett D A L, Lynd L R. Modeling simultaneous saccharification and fermentation of lignocellulose to ethanol in batch and continuous reactors[J]. Enzyme and Microbial Technology,1995,17:797-803
[132]张继泉,王瑞明,关凤梅.玉米秸杆同时糖化发酵生产燃料酒精的研究明[J].纤维素科学与技术,2002,10(3)：35-39
[133][124]张德强,张志毅,黄镇亚.木质纤维生物量一步法((SSF)转化成乙醇的研究(Ⅲ)[J].北京林业大学学报,2000,22(6)：50-54
[134]Saddler J N. Bioconversion of forest and agricultural plant residues [M]. Oxford:CAB 1993:1-352
[135]Tantirungkij M, Nakashima N, Seki T, et al. Construction of xylose-assimilating cerevisiae[J].J Ferment Bioeng,1993,75:83-88
[136]Wilson DB:Cellulases. In Encyclopedia of Microbiology[M],3rd edn. Edited by Schaechter M. San Diego:Elsever Inc; 2009.
[137]Saha, B.C., Lignocellulose biodegradation and applications in biotechnology[M]. In: Saha, B.C., Hayashi, K. (Eds.), Lignocellulose Biodegradation. American Chemical Society, Washington, DC,2004
[138]Saha, B.C., Freer, S.N., Bothast, R.J., Production, purification, and properties of a thermostable beta-glucosidase from a color variant strain of Aureobasidium pullulans[J]. Appl. Environ. Microbiol.1994; 60,3774-3780.
[139]Haki, G.D., Rakshit, S.K. Developments in industrially important thermostable enzymes:areview[J]. Bioresour. Technol.2003; 89,17-34.
[140]Han, Y., Chen, H. Characterization of β-glucosidase from corn stover and its application in simultaneous saccharification and fermentation[J]. Bioresour. Technol.2008; 99,6081-6087.
[141]Shen, Y., Zhang, Y., Ma, T., Bao, X., Du, F., Qu, Y., Simultaneous saccharification and fermentation of acid-pretreated corncobs with a recombinant Saccharomyces cerevisiae expressing beta-glucosidase [J]. Bioresour. Technol.2007,99:5099-5103.
[142]Joglekar A V, Karanth N C; Srinivasan M C, Significance of (β-D-glucosidase in the measurement of exo-β-D-glucanase activity of cellulolytic fungi[J]. Enzyme and Microbial Technology.1983,5(1):25-29
[143]Ong, L.G., Abd-Aziz, S., Noraini, S., Karim, M.I., Hassan, M.A., Enzyme production and profile by Aspergillus niger during solid substrate fermentation using palm kernel cake as substrate[J]. Appl. Biochem. Biotechnol.2004; 118,73-79.
[144]Rie, K., Makoto, Y., Tomomi, T., Kiyohiko, I., Tsuyoshi, O., Hiromichi, N., Masahiro, S. Production and characterization of recombinant Phanerochaete chrysosporium β-glucosidase in the methylotrophic yeast pichia pastoris[J]. Biosci. Biotechnol. Biochem 2003; 67(1):1-7.
[145]Beguin, P., Aubert, J. P. The biological degradation of cellulose[J]. FEMS Microbiol. Rev 1994; 13:25-58.
[146]Siegel, D., Ira, M., Mara, D., Ben-Ami, B., Shouming, H., Stephen, G., Withers, Oded, S. Cloning, Expression, Characterization, and Nucleophile Identification of Family 3. Aspergillus niger β-Glucosidase[J], J. Boil. Chem 2000; 275(7):4973-4980.
[147]Daniel, J., Daroit, Silvana, T., Silveira, Plinho, F., Hertz, Adriano, B. Production of extracellular β-glucosidase by Monascus purpureus on different growth substrates[J]. Process Biochem 2007; 42:904-908.
[148]Maicas, S., Mateo, J.J. Hydrolysis of terpenyl glycosides in grape juice and other fruit juices:a review[J]. Appl. Microbiol. Biotechnol 2005; 67:322-335.
[149]Zheng Z., Shetty K. Solid-state bioconversion of phenolics from cranberry pomace and role of Lentinus edodes β-glucosidase[J]. J. Agric. Food. Chem 2000; 48:895-900.
[150]Saha, B.C., Freer, S.N., Bothast, R.J., Production, purification, and properties of a thermostable β-glucosidase from a color variant strain of Aureobasidium pullulans[J], Appl. Environ. Microbiol.1994,60:3774-3780.
[151]Haki, G.D., Rakshit, S.K. Developments in industrially important thermostable enzymes:a review[J]. Bioresour. Technol.2003,89:17-34.
[152]Han, Y., Chen, H. Characterization of β-glucosidase from corn stover and its application in simultaneous saccharification and fermentation[J]. Bioresour. Technol.2008, 99:6081-6087
[153]Shen, Y., Zhang, Y., Ma, T., Bao, X., Du, F., Qu, Y., Simultaneous saccharification and fermentation of acid-pretreated corncobs with a recombinant Saccharomyces cerevisiae expressing beta-glucosidase[J]. Bioresour. Technol.2007,99:5099-5103.
[154]Daniel, J., Daroit, Silvana, T., Silveira, Plinho, F., Hertz, Adriano, B. Production of extracellular β-glucosidase by Monascus purpureus on different growth substrates. Process Biochem 2007[J],42:904-908.
[155]Martins, L.F., Kolling, D., Camassola, M., Dillon, A.J.P., Ramos, L.P. Comparison of Penicillium echinulatum and Trichoderma reesei cellulases in relation to their activity against various cellulosic substrates[J], Bioresour. Technol.2008,99:1417-1424.
[156]Stemberg, D. β-Glucosidase of Trichoderma:Its Biosynthesis and Role in Saccharification of Cellulose[J], Appl. Environ. Microb.1976,31:648-654.
[157]欧阳嘉,李鑫,王向明,严明,徐琳.纤维素酶结合域的研究进展[M].生物加工过程.2008,6(2)：10-14
[158]Ilan Levy, Oded Shoseyov. Cellulose-binding domains, Biotechnological applications[J], Biotechnology Advances 2002,20:191-213
[159]郑小玲,林陈水.微生物纤维素结合域研究及其在生物技术中的应用[M].纤维素科学与技术,2008,16(2)：66-72
[160]Elena S. Lymar, Bin L., V. Renganathan. Purification and Characterization of a Cellulose-Binding P-Glucosidase from Cellulose-Degrading Cultures of Phanerochaete chrysosporium[J], Applied and Environmental Microbiology,1995(8):2976-2980
[161]Bin L., V. Renganathan. Gene Cloning and Characterization of a Novel Cellulose-Binding β-Glucosidase from Phanerochaete chrysosporium[J], Applied and Environmental Microbiology,1998(7):2748-2754
[162]Makoto Yoshida, Tsuyoshi Ohira, Kiyohiko Igarashi, et. al., Production and characterization of recombinant Phanerochaete chrysosporium cellobiose dehydrogenase in the methylotrophic yeast Pichia pastoris[J], bioscience biotechnology biochemistry.2001, 65(9):2050-2057
[163]Ria Kawai, Makoto Yoshida, Tomomi Tani, et.al, Production and characterization of recombinant Phanerochaete chrysosporium β-glucosidase in the methylotrophic yeast Pichia pastoris[J], bioscience biotechnology biochemistry.2003,67(1):1-7
[164]Diana Ciolacu, Janez Kovac, Vanja Kokol. The effect of the cellulose-binding domain from Clostridium cellulovorans on the supramolecular structure of cellulose fibers[J], Carbohydrate Research.2010(345):621-630
[165]Yu-San Liu, Yining Zeng, Yonghua Luo, Qi Xu, Michael E. Himmel,Steve J. Smith, Shi-You Ding, Does the cellulose-binding module move on the cellulose surface? Cellulose[J],2009,16:587-597
[166]Gao, J., Weng, H., Zhu, D., Yuan, M., Guan, F., Xi, Y. Production and characterization of cellulolytic enzymes from the thermoacidophilic fungal Aspergillus terreus Mll under solid-state cultivation of corn stover[J]. Bioresour. Technol 2008; 99:7623-7629.
[167]Hsieh, M.C., Graham, T.L. Partial purification and characterization of a soybean β-glucosidase with high specific activity towards isoflavone conjugates[J]. Phytochemistry 2001; 58:995-1005.
[168]Sue, M., Ishihara, A., Iwamura, H. Purification and characterization of a β-glucosidase from rye (Secale cereale L.) seedlings[J]. Plant Sci 2000; 155:67-74.
[169]Kim, J.S., Lee, Y.Y., Torget, R.W. Cellulose Hydrolysis under Extremely Low Sulfuric Acid and High-Temperature Conditions[J]. Appl. Biochem. Biothec 2001,91:331-340.
[170]Daniel, J., Daroit, Silvana, T., Silveira, Plinho, F., Hertz, Adriano, B. Production of extracellular β-glucosidase by Monascus purpureus on different growth substrates [J]. Process Biochem 2007; 42:904-908.
[171]Maicas, S., Mateo, J.J. Hydrolysis of terpenyl glycosides in grape juice and other fruit juices:a review[J]. Appl. Microbiol. Biotechnol 2005; 67:322-335.
[172]Zheng Z., Shetty K. Solid-state bioconversion of phenolics from cranberry pomace and role of Lentinus edodes (3-glucosidase[J]. J. Agric. Food. Chem 2000; 48:895-900.
[173]Paula Gonzalez Pombo, Gabriel Perez, Franciso Carrau, et. al., One-step purification and characterization of an intracellular β-glucosidase from Metschnikowia pulcherrima[J], Biotechnol. Lett.,2008,30:1469-1475
[174]Yejun Han, Hongzhang Chen, Characterization of β-glucosidase from corn stover and its application in simultaneous saccharification and fermentation[J], Bioresource Technology 2008,99:6081-6087
[175]Eduardo, B.M., Adriane, S.G., Ivone, C., Tetrahedron α-and P-glucosidase inhibitors: chemical structure and biological activiry[J], Tetrahedron 2006,62:10277-10302.
[176]Takano, M., Moriyama, R., and Ohmiya, K. Structure of a β-glucosidase gene from Ruminococcus albus and properties of the translated product[J]. J. Ferment. Bioeng.1992,73: 79-88.
[177]Pandey, M. and Mishra, S. Cloning and expression of P-glucosidase gene from the yeast Pichia etchellsii[J]. J. Ferment. Bioeng,1995,80:446-453.
[178]Magalhaes PO, Ferraz A, Milagres AF. Enzymatic properties of two β-glucosidases from Ceriporiopsis subvermispora produced in biopulping conditions[J]. J Appl Microbiol 2006,101:480-486.
[179]Kaur J, Bhupinder SC, Badhan AK, Ghatora, Kaur S. Purification and characterization of β-glucosidase from Melanocarpus spMTCC 3922[J]. Electron J Biotechnol 2007, 10:261-70.
[180]Valaskova V, Baldrian P. Degradation of cellulose and hemicelluloses by the brown rot fungus Piptoporus betulinus-production of extracellular enzymes and characterization of themajor cellulases[J]. Microbiology 2006,152:3613-3622.
[181]Lymar ES, Li B, Renganathan V. Purification and characterization of a cellulosebinding β-glucosidase from cellulose-degrading cultures of Phanerochaete chrysosporium[J]. Appl Environ Microbiol 1995,61:2976-80.
[182]Ozaki H, Yamada K, Isolation of streptomyces sp. Producing glucose-tolerant β-glucosidase and properities of the enzyme[J]. Agri. Biol. Chem.,1992,55:979-987
[183]Li X, Calza R E. Purification and characterization of extracellularβ-glucosidase from the rumen fungus Neocallimastix frontalis EB 188[J], Enzyme Microb Technol.,1991, 13:622-628
[184]Rie Kaiwai, Makoto Yoshida, Tomomi Tani, et. al, Production and characterization of recombinant Phanerochaete chrysosporium β-Glucosidase in the Methylotrophic Yeast Pichia pastoris[J], Biosci. Biotechnol. Biochem.,2003,67(1):1-7
[185]Vasanti Deshpande, Karl-Erik Eriksson, and Bert Pettersson, Production, Purification and Partial Characterization of 1,4-β-glucosidase Enzymes from Sporotrichum pulverulentum[J], Eur. J. Biochem.1978,90:191-198
[186]Elena S. Lymar, Bin L, V. Renganathan, Purification and Characterization of a Cellulose-Binding P-Glucosidase from Cellulose-Degrading Cultures of Phanerochaete chrysosporium[J], Applied and Environment Microbiology,1995,61(8):2976-2980
[187]Ghose T K. Measurement of cellulase activities[J]. Pure Appl Chem,1987,59 (2): 257-268.
[188]Claeyssens, M., Aerts, G., Characterization of cellulolytic activities in commercial Trichoderma reesei preparations:an approach using small, chromogenic substrates[J]. Bioresour. Technol.1992,39,143-146.
[189]Ghose, T.K., Measurement of cellulase activities[J]. Pure Appl. Chem.1986,59, 257-268.
[190]Bailey, M.J., Biely, P., Poutanen, K., Interlaboratory testing of methods for assay of xylanase activity[J]. J. Biotechnol.1992,23:257-270.
[191]彭汀汀,董宏平,彭惠等,一株具木聚糖酶活链霉菌的鉴定及其木聚糖降解酶系分析[M],南京师大学报(自然科学版),2006,29(4)：73-78
[192]Duff, S. J. B. and W. D. Murray. Bioconversion of forest products industry waste cellulosics to fuel ethanol:Areview[J]. Bioresource Technology 1996,55:1-33.
[193]Marimuthu Jeya, Ye-Wang Zhang, In-Won Kim, et, al. Enhanced saccharification of alkali-treated rice straw by cellulase from Trametes hirsuta and statistical optimization of hydrolysis conditions by RSM[J]., Bioresource Technology 2009 (100):5155-5161
[194]Chen, H., Liu, L., Unpolluted fractionation of wheat straw by steam explosion and ethanol extraction[J]. Bioresour. Technol.2007,98,666-676.
[195]Chang VS, Burr B, Holtzapple MT. Lime pretreatment of switchgrass[J]. Appl. Biochem. Biotechnol.1997,63(65):3-19.
[196]Chang VS, Nagwani M, Holtzapple MT. Lime pretreatment of crop residues:bagasse and wheat straw[J]. Appl. Biochem. Biotechnol.1998,74:135-159.
[197]刘书钗.制浆造纸分析与检测[M].化学工业出版社,2003：17-31.
[198]Agu, R.C., Amadife, A.E., Ude, C.M., Onyia, A., Ogu, E.O., Okafor, M., Ezejiofor, E., 1997. Combined heat treatment and acid hydrolysis of cassava grate waste (CGW) biomass for ethanol production[M]. Waste Manage. (Oxford) 17,91-96.
[199]Liu, S.C., Analysis and Measurement in Papermaking Industry[M]. Chemical Industry Press, Beijing.2004:19-27.
[200]S. Hari Krishna, K. Prasanthi, G. V. Chowdary and C. Ayyanna, Simultaneous saccharification and fermentation of pretreated sugar cane leaves to ethanol[J], Process Biochemistry,1998,33(8):825-830,
[201]Yejun Han, Hongzhang Chen, Characterization of b-glucosidase from corn stover and its application in simultaneous saccharification and fermentation[J], Bioresource Technology 2008(99):6081-6087
[202]Takagi, M., Abe, S., Suzuki, S., Emert, G. H. and Yara, N., A method for production of alcohol directly from cellulose using cellulase and yeast. In Proceedings of Bioeonversion of Celhdosie Substances into Energy[J], Chemicals and Microbial Protein, ed. T. K. Ghose. J.I.T., Delhi,1977.551-571.
[203]Krishna, S.H., Reddy, T.J., Chowdary, G.V., Simultaneous saccharification and fermentation of lignocellulosic wastes to ethanol using a thermotolerant yeast[J], Bioresour. Technol.2001,77:193-196.
[204]Shen, Y., Zhang, Y., Ma, T., Bao, X., Du, F., Qu, Y., Simultaneous saccharification and fermentation of acid-pretreated corncobs with a recombinant Saccharomyces cerevisiae expressing beta-glucosidase[J]. Bioresour. Technol.2007,99:5099-5103.
[205]Sue, M., Ishihara, A., Iwamura, H., Purification and characterization of a b-glucosidase from rye (Secale cereale L.) seedlings[J]. Plant Sci.2000,155:67-74.
[206]Xiao, Z., Zhang, X., Gregg, D., Saddler, J.N., Effects of sugar inhibition on cellulases and b-glucosidase during enzymatic hydrolysis of softwood substrates[J]. Appl. Biochem. Biotechnol.2004,115:1115-1126.
[207]Chen, M., Zhao, J., Xia, L., Enzymatic hydrolysis of maize straw polysaccharides for the production of reducing sugars[J]. Carbohyd. Polym.2008,71:411-415
[208]Saha, B.C., Cotta, M.A., Lime pretreatment, enzymatic saccharification and fermentation of rice hulls to ethanol[J]. Biomass Bioenergy 2008,32:971-977.
[209]Adsul, M.G, Bastawde, K.B., Varma, A.J., Gokhale, D.V., Strain improvement of Penicillium janthinellum NCIM 1171 for increased cellulase production[J]. Bioresour. Technol.2007,98:1467-1473.
[210]Zhang, Q., Cai, W., Enzymatic hydrolysis of alkali-pretreated rice straw by Trichoderma reesei ZM4-F3[J], Biomass Bioenergy 2008,32:1130-1135.
[211]Saha, B.C., Iten, L.B., Cotta, M.A., Wu, Y.V., Dilute acid pretreatment, enzymatic saccharification and fermentation of wheat straw to ethanol[J]. Process Biochem.2005,40: 3693-3700.
[212]Kaar, W.E., Gutierrez, C.V., Kinoshita. C.M., Steam explosion of sugarcane bagasse as a pretreatment for conversion to ethanol[J]. Biomass Bioenergy.1998,14:277-287.
[213]Vlasenko, E.Y., Ding, H., Labavitch, J.M., Shoemaker, S.P., Enzymatic hydrolysis of pretreated rice straw[J]. Bioresour. Technol.1997,59:109-119.
[214]Marimuthu Jeya, Ye-Wang Zhang, In-Won Kim, Jung-Kul Lee. Enhanced saccharification of alkali-treated rice straw by cellulase from Trametes hirsuta and statistical optimization of hydrolysis conditions by RSM[J], Bioresource Technology 2009,100: 5155-5161