酒类酒球菌SD-2a和31MBR的β-D-葡萄糖苷酶研究
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摘要
优质葡萄酒不仅表现在外观、口感等方面，更体现在香气方面，香气是影响葡萄酒质量的关键因素之一。在葡萄酒酿造中，酒类酒球菌产生的β-D-葡萄糖苷酶是降解糖苷类物质产生挥发性香气物质的关键酶。酒类酒球菌SD-2a和31MBR是两株优良的葡萄酒酿造乳酸菌，具有良好的苹果酸乳酸发酵性能。研究这两株菌的β-D-葡萄糖苷酶活性对增加葡萄酒香气，提高葡萄酒整体质量具有十分重要的意义。
本论文首先利用合成底物采用比色法对SD-2a和31MBR的β-D-葡萄糖苷酶进行了检测、定位和特性研究；在此基础上，又利用自然底物在缓冲液和模拟酒中评价了这两株菌对糖苷的降解能力；最后，利用分子生物学技术对这两株菌的β-D-葡萄糖苷酶基因进行了克隆、测序、生物信息学分析及基因表达量分析，主要研究结果如下：
（1）ATB培养基比MRST培养基更适于做酒类酒球菌SD-2a和31MBR的生长培养基，SD-2a和31MBR在ATB培养基中都具有β-D-葡萄糖苷酶活性，且SD-2a的酶活显著高于31MBR。
（2）利用合成底物进行酶活定位试验得到，SD-2a完整细胞具有较高酶活，而31MBR破碎液具有较高酶活；这两株菌的β-D-葡萄糖苷酶都为胞内酶，这些胞内酶大部分为可溶性蛋白，主要存在于细胞质液和周质腔中，部分为不溶性蛋白，存在于原生质体的膜结构上。酶活诱导试验表明，SD-2a和31MBR的β-D-葡萄糖苷酶为组成型酶，在纤维二糖和熊果苷的诱导下，酶位置基本不发生变化，但不同部位的酶活有一定程度的变化。
（3）利用合成底物研究了酿酒条件及其胁迫对SD-2a和31MBR β-D-葡萄糖苷酶活性的影响，结果显示：胁迫对这两株菌酶活的影响较小；在酿酒条件下，这两株菌β-D-葡萄糖苷酶粗酶液的活性均较低，而SD-2a完整细胞在酿酒条件下仍具有一定的酶活。
（4）利用从葡萄中分离出来的糖苷物质研究了SD-2a和31MBR对糖苷的降解能力，结果显示：在pH5.0缓冲液中，和SD-2a相比，31MBR产生更多的葡萄糖糖基；而在模拟酒中，SD-2a降解自然糖苷产生的挥发性物质无论是种类还是含量都显著高于31MBR，对香气的影响更显著于31MBR，说明SD-2a具有更强的糖苷降解能力。
（5）利用分子生物学技术从SD-2a和31MBR中成功克隆出了5个葡萄糖苷酶基因，其中OEOE-1569编码β-D-葡萄糖苷酶，其余4个编码6-磷酸-β-葡萄糖苷酶；测序结果显示，基因OEOE-1210、OEOE-1569和OEOE-0224编码的蛋白序列与已报道的蛋白序列具有较高同源性，达99%以上；生物信息学分析显示这三个基因编码的葡萄糖苷酶为可溶性酶，主要存在于细胞质液中。
（6）利用qRT-PCR技术对SD-2a和31MBR的5个葡萄糖苷酶基因进行了表达量分析，结果表明：编码β-D-葡萄糖苷酶的基因OEOE-1569与SD-2a和31MBR胞内β-D-葡萄糖苷酶酶活相关，编码6-磷酸-β-葡萄糖苷酶的基因OEOE-0224与这两株菌完整细胞β-D-葡萄糖苷酶酶活相关；验证了“碳代谢抑制”理论，从一定程度上揭示了基因OEOE-0224编码的磷酸烯醇式丙酮酸转移酶系统中的6-磷酸-β-葡萄糖苷酶是SD-2a完整细胞具有β-D-葡萄糖苷酶活性的原因。
Flavor is one important factor to high quality wine. In addition to the initial impact thatwine color and taste have on the perception of wine quality, it is the aroma and flavor that hasthe greatest impact on consumers. β-D-glucosidase derived from Oenococcus oeni strains isthe most important glycosidase to hydrolyze glycosylated aroma precursors, releasing activearoma and flavor compounds, during malolactic fermentation (MLF). O. oeni SD-2a and31MBR are two excellent bacteria used in winemaking, possessing important oenologicalcharacteristics, particularly, being able to perform MLF effectively in winery conditions. Thus,investigating β-D-glucosidase of the two strains is of great significance for aromaenhancement and wine quality improvement in winemaking.
In the present study, β-D-glucosidase activity of SD-2a and31MBR was detected,localized and characterized spectrophotometrically with synthetic substrate p-nitrophenylβ-D-glucopyranoside firstly. Then the ability of the two strains to hydrolyze glycosides wasalso evaluated with natural substrate extracted from grape in buffer and model wine. Finally,β-D-glucosidase genes of both strains were cloned, sequenced and characterized throughbioinformatic analysis, and the gene expression was analyzed with qRT-PCR technology. Themain results are as following.
(1) Compared with MRST medium, ATB medium was preferable for O. oeni SD-2a and31MBR growth. Enzyme assay with synthetic substrate showed both SD-2a and31MBRpossessed β-D-glucosidase activity in ATB medium, with SD-2a showing higher activity than31MBR.
(2) Enzyme localization assay showed31MBR possessed higher total enzyme activitythan that of SD-2a, while SD-2a showed higher whole cells activity; β-D-glucosidase wasintracellular form for both strains, most of which was soluble protein existing in cytoplasmand periplasm, and some was insoluble existing in protoplast membrane. Enzyme inductionassay exhibited β-D-glucosidase of the two strains was constitutive, however, varied enzymeactivities were observed when bacteria was cultured with arbutin or cellobiose.
(3) The influence of winelike conditions and abiotic stress on β-D-glucosidase activity ofSD-2a and31MBR was conducted with synthetic substrate. Abiotic stress showed less effect on β-D-glucosidase activity of the two strains; crude β-D-glucosidase of both strains showedlittle activity under winelike conditions, while whole cells of SD-2a remained high activityunder such conditions.
(4) The ability of SD-2a and31MBR to hydrolyze glycosides was also evaluated withnatural substrate extracted from grape. More glycosyl-glucose was detected for31MBR thanSD-2a in pH5.0buffer system; while in model wine system, more volatiles, whether onvariety or on content, was detected for SD-2a than31MBR, SD-2a proved possessing higherenzyme activity and preferable than31MBR for aroma enhancement during winemaking.
(5) Five glucosidase genes were cloned from both SD-2a and31MBR, OEOE-1569coding for β-D-glucosidase and the others coding for6-P-β-glucosidase. Deduced amino acidsequences of sequenced genes OEOE-1210OEOE-1569and OEOE-0224showed highhomology (>99%) to the reported protein sequense in NCBI. Bioinformatic analysis showedthe glucosidases coded by these three genes were soluble protein, existing mainly incytoplasm.
(6) The expression of five glucosidase genes cloned from both SD-2a and31MBR wasanalyzed with qRT-PCR technology. Gene OEOE-1569coding for β-D-glucosidase wasrelated to the intracellular β-D-glucosidase activity of the two strains, while gene OEOE-0224coding for6-P-β-glucosidase was related to whole cells β-D-glucosidase activity of bothstrains. The result confirmed the theory of carbon catabolite repression, and to some extentproved it is phosphoenolpyruvate dependent phospho transferase system (PEP-PTS) and6-P-β-glucosidase coded by gene OEOE-0224that contributes to whole cells β-D-glucosidaseactivity of SD-2a.
本论文首先利用合成底物采用比色法对SD-2a和31MBR的β-D-葡萄糖苷酶进行了检测、定位和特性研究；在此基础上，又利用自然底物在缓冲液和模拟酒中评价了这两株菌对糖苷的降解能力；最后，利用分子生物学技术对这两株菌的β-D-葡萄糖苷酶基因进行了克隆、测序、生物信息学分析及基因表达量分析，主要研究结果如下：
（1）ATB培养基比MRST培养基更适于做酒类酒球菌SD-2a和31MBR的生长培养基，SD-2a和31MBR在ATB培养基中都具有β-D-葡萄糖苷酶活性，且SD-2a的酶活显著高于31MBR。
（2）利用合成底物进行酶活定位试验得到，SD-2a完整细胞具有较高酶活，而31MBR破碎液具有较高酶活；这两株菌的β-D-葡萄糖苷酶都为胞内酶，这些胞内酶大部分为可溶性蛋白，主要存在于细胞质液和周质腔中，部分为不溶性蛋白，存在于原生质体的膜结构上。酶活诱导试验表明，SD-2a和31MBR的β-D-葡萄糖苷酶为组成型酶，在纤维二糖和熊果苷的诱导下，酶位置基本不发生变化，但不同部位的酶活有一定程度的变化。
（3）利用合成底物研究了酿酒条件及其胁迫对SD-2a和31MBR β-D-葡萄糖苷酶活性的影响，结果显示：胁迫对这两株菌酶活的影响较小；在酿酒条件下，这两株菌β-D-葡萄糖苷酶粗酶液的活性均较低，而SD-2a完整细胞在酿酒条件下仍具有一定的酶活。
（4）利用从葡萄中分离出来的糖苷物质研究了SD-2a和31MBR对糖苷的降解能力，结果显示：在pH5.0缓冲液中，和SD-2a相比，31MBR产生更多的葡萄糖糖基；而在模拟酒中，SD-2a降解自然糖苷产生的挥发性物质无论是种类还是含量都显著高于31MBR，对香气的影响更显著于31MBR，说明SD-2a具有更强的糖苷降解能力。
（5）利用分子生物学技术从SD-2a和31MBR中成功克隆出了5个葡萄糖苷酶基因，其中OEOE-1569编码β-D-葡萄糖苷酶，其余4个编码6-磷酸-β-葡萄糖苷酶；测序结果显示，基因OEOE-1210、OEOE-1569和OEOE-0224编码的蛋白序列与已报道的蛋白序列具有较高同源性，达99%以上；生物信息学分析显示这三个基因编码的葡萄糖苷酶为可溶性酶，主要存在于细胞质液中。
（6）利用qRT-PCR技术对SD-2a和31MBR的5个葡萄糖苷酶基因进行了表达量分析，结果表明：编码β-D-葡萄糖苷酶的基因OEOE-1569与SD-2a和31MBR胞内β-D-葡萄糖苷酶酶活相关，编码6-磷酸-β-葡萄糖苷酶的基因OEOE-0224与这两株菌完整细胞β-D-葡萄糖苷酶酶活相关；验证了“碳代谢抑制”理论，从一定程度上揭示了基因OEOE-0224编码的磷酸烯醇式丙酮酸转移酶系统中的6-磷酸-β-葡萄糖苷酶是SD-2a完整细胞具有β-D-葡萄糖苷酶活性的原因。
Flavor is one important factor to high quality wine. In addition to the initial impact thatwine color and taste have on the perception of wine quality, it is the aroma and flavor that hasthe greatest impact on consumers. β-D-glucosidase derived from Oenococcus oeni strains isthe most important glycosidase to hydrolyze glycosylated aroma precursors, releasing activearoma and flavor compounds, during malolactic fermentation (MLF). O. oeni SD-2a and31MBR are two excellent bacteria used in winemaking, possessing important oenologicalcharacteristics, particularly, being able to perform MLF effectively in winery conditions. Thus,investigating β-D-glucosidase of the two strains is of great significance for aromaenhancement and wine quality improvement in winemaking.
In the present study, β-D-glucosidase activity of SD-2a and31MBR was detected,localized and characterized spectrophotometrically with synthetic substrate p-nitrophenylβ-D-glucopyranoside firstly. Then the ability of the two strains to hydrolyze glycosides wasalso evaluated with natural substrate extracted from grape in buffer and model wine. Finally,β-D-glucosidase genes of both strains were cloned, sequenced and characterized throughbioinformatic analysis, and the gene expression was analyzed with qRT-PCR technology. Themain results are as following.
(1) Compared with MRST medium, ATB medium was preferable for O. oeni SD-2a and31MBR growth. Enzyme assay with synthetic substrate showed both SD-2a and31MBRpossessed β-D-glucosidase activity in ATB medium, with SD-2a showing higher activity than31MBR.
(2) Enzyme localization assay showed31MBR possessed higher total enzyme activitythan that of SD-2a, while SD-2a showed higher whole cells activity; β-D-glucosidase wasintracellular form for both strains, most of which was soluble protein existing in cytoplasmand periplasm, and some was insoluble existing in protoplast membrane. Enzyme inductionassay exhibited β-D-glucosidase of the two strains was constitutive, however, varied enzymeactivities were observed when bacteria was cultured with arbutin or cellobiose.
(3) The influence of winelike conditions and abiotic stress on β-D-glucosidase activity ofSD-2a and31MBR was conducted with synthetic substrate. Abiotic stress showed less effect on β-D-glucosidase activity of the two strains; crude β-D-glucosidase of both strains showedlittle activity under winelike conditions, while whole cells of SD-2a remained high activityunder such conditions.
(4) The ability of SD-2a and31MBR to hydrolyze glycosides was also evaluated withnatural substrate extracted from grape. More glycosyl-glucose was detected for31MBR thanSD-2a in pH5.0buffer system; while in model wine system, more volatiles, whether onvariety or on content, was detected for SD-2a than31MBR, SD-2a proved possessing higherenzyme activity and preferable than31MBR for aroma enhancement during winemaking.
(5) Five glucosidase genes were cloned from both SD-2a and31MBR, OEOE-1569coding for β-D-glucosidase and the others coding for6-P-β-glucosidase. Deduced amino acidsequences of sequenced genes OEOE-1210OEOE-1569and OEOE-0224showed highhomology (>99%) to the reported protein sequense in NCBI. Bioinformatic analysis showedthe glucosidases coded by these three genes were soluble protein, existing mainly incytoplasm.
(6) The expression of five glucosidase genes cloned from both SD-2a and31MBR wasanalyzed with qRT-PCR technology. Gene OEOE-1569coding for β-D-glucosidase wasrelated to the intracellular β-D-glucosidase activity of the two strains, while gene OEOE-0224coding for6-P-β-glucosidase was related to whole cells β-D-glucosidase activity of bothstrains. The result confirmed the theory of carbon catabolite repression, and to some extentproved it is phosphoenolpyruvate dependent phospho transferase system (PEP-PTS) and6-P-β-glucosidase coded by gene OEOE-0224that contributes to whole cells β-D-glucosidaseactivity of SD-2a.
引文
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