中性植酸酶产生菌的筛选及基因工程菌的构建
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摘要
中性植酸酶不仅具有较好的热稳定性,有助于抵抗饲料制粒过程中高温引起的酶失活,而且其酶促反应最适pH在7.0-7.5之间,可有效弥补酸性植酸酶的不足。本研究筛选了中性植酸酶产生菌,优化了其液态产酶参数,克隆与分析了其基因,在此基础上,构建了中性植酸酶原核和真核表达基因工程菌,旨在为中性植酸酶产品的工业化生产奠定基础。主要结果如下：
1.中性植酸酶产生菌的筛选、鉴定及其液态产酶参数优化
通过平板初筛和摇瓶复筛,从土壤中筛选出6株能够分泌中性植酸酶的菌株,其中菌株ZJ-6显示较高的活力。经鉴定表明,菌株ZJ-6为地衣芽孢杆菌,其液态发酵产酶培养基中最佳碳源为l%葡萄糖,氮源为0.1%硫酸铵,初始pH为7.5,最佳培养温度为55℃。经36h培养后,产酶水平达到最高,酶活为0.267U/ml,比活为0.701U/mmg。
2.地衣芽孢杆菌ZJ-6中性植酸酶基因克隆及序列分析
通过PCR对地衣芽孢杆菌ZJ-6中性植酸酶基因(phyC)进行扩增,获得一段长约1.2kb的特异性产物,并将其克隆到pUCmT载体,构建含有目的基因片段的重组质粒pUCm-T phyC。序列分析表明,phyC基因全长1146bp,编码381个氨基酸,5’端有一段编码31个氨基酸的信号肽序列；不含有酸性植酸酶蛋白中均存在的高度保守的RHGXRXP和HD序列；与已报道的地衣芽孢杆菌(AY651979)、凝结芽孢杆菌(DQ346195)、枯草芽孢杆菌(AJ277890)、淀粉液化芽孢杆菌(AY836773)和芽孢杆菌sp.DSl1(BSU85968)中性植酸酶核苷酸同源性分别为99%、70%、67%、67%和67%,与所编码蛋白同源性分别为99%、69%、65%、65%和64%。该酶蛋白成熟肽二级结构中无规卷曲占57.42%,折叠占40.29%,α-螺旋占2.29%；其三级结构与模板蛋白lh61A(1.8A)同源性为68.2%。
3.中性植酸酶基因工程菌株的构建
将地衣芽孢杆菌ZJ-6编码的中性植酸酶基因(phyC)定向插入到原核表达载体pET-30a(+)上,获得的重组质粒phyC-pET-30a(+)在大肠杆菌BL21(DE3)中表达,表达产物(EPhyC5)经Ni-NTA亲和层析纯化后比活为2.87U／mg。SDS-PAGE表明,EPhyC5相对分子量为42.86 kDa。
将地衣芽孢杆菌ZJ-6中性植酸酶成熟肽基因(phyCm)以N-端融合方式插入到酵母表达载体pPIC9K上的α-因子信号肽编码序列的3’端,构建重组质粒pPIC9K-phyCm,电击法转化毕赤氏酵母GS1 15。经MD／MM平板筛选、G418抗性筛选和酶活性测定,获得20个阳性表达子(pPhyCm),其中pPhyCm6活性最高。将pPhyCm6接种于BMMY培养基中,经0.5%甲醇诱导培养96h,发酵上清液中重组中性植酸酶(PPhyCm6)比活为8.64U／mmg。SDS-PAGE结果表明,PPhyCm6相对分子量为38.78kDa,与理论推算的分子量(38.7kDa)相吻合。在巴斯德毕赤氏酵母中实现了有生物学活性中性植酸酶的分泌表达。
4.重组酶及其亲本酶的酶学性质分析
野生酶PhyC最适温度和最适pH分别为55℃和7.0；在80℃、pH7.0条件下处理10 min,残余酶活为57.36%；在pH6.5-9.0,25℃条件下处理1h,残余酶活均高于80%。EPhyC5最适温度和最适pH分别为60℃和7.0；在80℃、pH7.0条件下处理10 min,残余酶活为68.26%；在pH6.0-9.0,25℃条件下处理1h,残余酶活均高于80%。PPhyCm6最适温度和最适pH分别为60℃和7.5；在80℃、pH7.5条件下处理2 min,残余酶活为59.42%；在pH5.0-9.0,25℃条件下处理1h,残余酶活均高于80%。
重组酶EPhyC5和PPhyCm6在离子影响、底物特异性和Ca2+依赖性方面与亲本酶PhyC基本一致。EDTA、Cu2+、Cd2+、Ba2+和Mn2+对酶活性均有显著抑制作用；1.0mmol/LCa2+能提高酶蛋白的热稳定性和pH稳定性；植酸钠是特异性作用底物；氟化钠和钒酸铵均能引起酶活性降低。酶学性质
Neutral phytases, which exhibit their desirable activity profile at neutral pH, good thermal stability and strict substrate specificity for the calcium-phytate complex and produce myo-inositol trisphosphate as the final product, have considerable potential in commercial and environmental applications. This investigation aims to screen out the neutral phytase-producing strains, optimize the fermentation parameters and clone the neutral phytase gene. On these bases, the further study aims to construct engineered strains producing neutral phytase for the industrialized production. The main results were listed as follows:
1. Screening, identification and fermentation parameters of neutral phytase producing strains
A wild type strain of neutral phytate-degrading bacteria was isolated from soil samples of Zhejiang province, and identified as Bacillus licheniformis ZJ-6 according to the morphological, physico-chemical properties and 16S rRNA sequences analysis. The optimal fermentation parameters for producing neutral phytase by strain ZJ-6 were determined by single factor test and the results were as follows:1.0% dextrose used as carbon source,0.1%(NH4)SO4 as nitrogen source, initially pH7.5, incubation temperature 55℃. After incubation for 36h under these conditions, the activity of neutral phytase reached 0.267 U/ml with specific activity 0.701U/mg.
2. Sequence analyses of the neutral phytase gene from B.licheniformis ZJ-6
The phyC gene encoding the neutral phytase of B.licheniformis ZJ-6 was amplified by polymerase chain reaction (PCR) with designed primers according to the sequences of phytase genes from Bacillus. The amplified fragment was cloned into the vector pUCm-T. Sequencing results showed that the coding region was 1146 bp in size encoding a peptide of 381 amino acid residues, in which there were a signal peptide of 31 amino acids and a mature peptide of 350 amino acids. The deduced amino acid sequence of phyC showed significant similarity to the reported sequences of other neutral phytases from Bacillus. Moreover, it did not display the active site hepta-peptide motif RHGXRXP or the catalytically active dipeptide HD in acidic phytases. The mature protein of the PhyC had random coil (57.42%), extended strand (40.29%) and alpha helix (2.29%). The 3-D structure of the phyC was predicted by homologous modeling technology, the results indicated that the homology was 68.2% between the template protein (1h61 A) and the mature peptide of the phyC.
3. The construction of neutral phytase-producing engineered strains
The gene encoding B.licheniformis ZJ-6 neutral phytase (phyC) was cloned from vector pUCm-T phyCl by PCR. The phyC with original signal peptide was ligated into expression vector pET-30a(+) and transformed into Escherichia coli BL21 (DE3). The phyC was successfully expressed and the product, EPhyC5, was purified by Ni-NTA chromatography. The activity of purified EPhyC5 was 2.87U/mg. SDS-PAGE analysis showed that molecular mass of the purified EPhyC5 was 42.86kDa, which was similar to the the theory molecular mass,42.1 kDa.
The phyCm fragment encoding the mature peptide sequence of B.licheniformis ZJ-6 neutral phytase was amplified and cloned into expression vector pPIC9K. The pPIC9K-phyCm plasmid was linearized and transformed into Pichia Pastoris GS115 strain by electroporation. Positive strain was screened and purified by culturing on MD/MM plate and G418. After 96h 0.5% methanol induction, the activity of recombinant phytase (PPhyCm6) in culture supernatant of pPhyCm6 transformant was 8.64 U/mg. SDS-PAGE analysis showed that the molecular mass of PPhyCm6 was 38.78 kDa, which was in good agreement with the theory molecular mass, 38.7kDa.
4. Analyses of enzymatic properties of PhyC, EPhyC5 and PPhyCm6
The optimum temperature and pH of the PhyC were 55℃and 7.0, respectively. After treated at 80℃, pH 7.0 for 10 min, the residual activity of PhyC was 57.36%. Over 80% of PhyC activity was retained after treatment of the enzyme by preincubation over a pH range of 6.5-9.0 for 1 h at 25℃.
The optimum temperature and pH of the EPhyC5 were 60℃and 7.0, respectively. After treated at 80℃, pH 7.0 for 10 min, the residual activity of EPhyC5 was 68.26%. Over 80% of EPhyC5 activity was kept after treatment of the enzyme by preincubated over a pH range of 6.0-9.0 for 1 h at 25℃.
The optimum temperature and pH of the PPhyCm6 were 60℃and 7.5, respectively. After treated at 80℃, pH 7.5 for 10 min, the residual activity of PPhyCm6 was 59.42%. Over 80% of PPhyCm6 activity was retained after the enzyme treated by preincubation over a pH range of 5.0-9.0 for 1 h at 25℃.
The others enzymatic properties of the recombinant neutral phytase (EPhyC5 and PPhyCm6) were identical to those of the original enzyme. PhyC, EPhyC5 and PPhyCm6 were greatly inhibited by EDTA and metal ions such as Cd2+, Mn2+, Cu2+ and Ba2+. Their thermostabilities and pH stabilities could be improved in the presence of 1mmol/L Ca2+. All of them exhibit highly strict substrate specificity for sodium phytate and had no enzymatic activity on other phosphate esters tested. NaF and vanadate showed slight inhibition on their activities.
1.中性植酸酶产生菌的筛选、鉴定及其液态产酶参数优化
通过平板初筛和摇瓶复筛,从土壤中筛选出6株能够分泌中性植酸酶的菌株,其中菌株ZJ-6显示较高的活力。经鉴定表明,菌株ZJ-6为地衣芽孢杆菌,其液态发酵产酶培养基中最佳碳源为l%葡萄糖,氮源为0.1%硫酸铵,初始pH为7.5,最佳培养温度为55℃。经36h培养后,产酶水平达到最高,酶活为0.267U/ml,比活为0.701U/mmg。
2.地衣芽孢杆菌ZJ-6中性植酸酶基因克隆及序列分析
通过PCR对地衣芽孢杆菌ZJ-6中性植酸酶基因(phyC)进行扩增,获得一段长约1.2kb的特异性产物,并将其克隆到pUCmT载体,构建含有目的基因片段的重组质粒pUCm-T phyC。序列分析表明,phyC基因全长1146bp,编码381个氨基酸,5’端有一段编码31个氨基酸的信号肽序列；不含有酸性植酸酶蛋白中均存在的高度保守的RHGXRXP和HD序列；与已报道的地衣芽孢杆菌(AY651979)、凝结芽孢杆菌(DQ346195)、枯草芽孢杆菌(AJ277890)、淀粉液化芽孢杆菌(AY836773)和芽孢杆菌sp.DSl1(BSU85968)中性植酸酶核苷酸同源性分别为99%、70%、67%、67%和67%,与所编码蛋白同源性分别为99%、69%、65%、65%和64%。该酶蛋白成熟肽二级结构中无规卷曲占57.42%,折叠占40.29%,α-螺旋占2.29%；其三级结构与模板蛋白lh61A(1.8A)同源性为68.2%。
3.中性植酸酶基因工程菌株的构建
将地衣芽孢杆菌ZJ-6编码的中性植酸酶基因(phyC)定向插入到原核表达载体pET-30a(+)上,获得的重组质粒phyC-pET-30a(+)在大肠杆菌BL21(DE3)中表达,表达产物(EPhyC5)经Ni-NTA亲和层析纯化后比活为2.87U／mg。SDS-PAGE表明,EPhyC5相对分子量为42.86 kDa。
将地衣芽孢杆菌ZJ-6中性植酸酶成熟肽基因(phyCm)以N-端融合方式插入到酵母表达载体pPIC9K上的α-因子信号肽编码序列的3’端,构建重组质粒pPIC9K-phyCm,电击法转化毕赤氏酵母GS1 15。经MD／MM平板筛选、G418抗性筛选和酶活性测定,获得20个阳性表达子(pPhyCm),其中pPhyCm6活性最高。将pPhyCm6接种于BMMY培养基中,经0.5%甲醇诱导培养96h,发酵上清液中重组中性植酸酶(PPhyCm6)比活为8.64U／mmg。SDS-PAGE结果表明,PPhyCm6相对分子量为38.78kDa,与理论推算的分子量(38.7kDa)相吻合。在巴斯德毕赤氏酵母中实现了有生物学活性中性植酸酶的分泌表达。
4.重组酶及其亲本酶的酶学性质分析
野生酶PhyC最适温度和最适pH分别为55℃和7.0；在80℃、pH7.0条件下处理10 min,残余酶活为57.36%；在pH6.5-9.0,25℃条件下处理1h,残余酶活均高于80%。EPhyC5最适温度和最适pH分别为60℃和7.0；在80℃、pH7.0条件下处理10 min,残余酶活为68.26%；在pH6.0-9.0,25℃条件下处理1h,残余酶活均高于80%。PPhyCm6最适温度和最适pH分别为60℃和7.5；在80℃、pH7.5条件下处理2 min,残余酶活为59.42%；在pH5.0-9.0,25℃条件下处理1h,残余酶活均高于80%。
重组酶EPhyC5和PPhyCm6在离子影响、底物特异性和Ca2+依赖性方面与亲本酶PhyC基本一致。EDTA、Cu2+、Cd2+、Ba2+和Mn2+对酶活性均有显著抑制作用；1.0mmol/LCa2+能提高酶蛋白的热稳定性和pH稳定性；植酸钠是特异性作用底物；氟化钠和钒酸铵均能引起酶活性降低。酶学性质
Neutral phytases, which exhibit their desirable activity profile at neutral pH, good thermal stability and strict substrate specificity for the calcium-phytate complex and produce myo-inositol trisphosphate as the final product, have considerable potential in commercial and environmental applications. This investigation aims to screen out the neutral phytase-producing strains, optimize the fermentation parameters and clone the neutral phytase gene. On these bases, the further study aims to construct engineered strains producing neutral phytase for the industrialized production. The main results were listed as follows:
1. Screening, identification and fermentation parameters of neutral phytase producing strains
A wild type strain of neutral phytate-degrading bacteria was isolated from soil samples of Zhejiang province, and identified as Bacillus licheniformis ZJ-6 according to the morphological, physico-chemical properties and 16S rRNA sequences analysis. The optimal fermentation parameters for producing neutral phytase by strain ZJ-6 were determined by single factor test and the results were as follows:1.0% dextrose used as carbon source,0.1%(NH4)SO4 as nitrogen source, initially pH7.5, incubation temperature 55℃. After incubation for 36h under these conditions, the activity of neutral phytase reached 0.267 U/ml with specific activity 0.701U/mg.
2. Sequence analyses of the neutral phytase gene from B.licheniformis ZJ-6
The phyC gene encoding the neutral phytase of B.licheniformis ZJ-6 was amplified by polymerase chain reaction (PCR) with designed primers according to the sequences of phytase genes from Bacillus. The amplified fragment was cloned into the vector pUCm-T. Sequencing results showed that the coding region was 1146 bp in size encoding a peptide of 381 amino acid residues, in which there were a signal peptide of 31 amino acids and a mature peptide of 350 amino acids. The deduced amino acid sequence of phyC showed significant similarity to the reported sequences of other neutral phytases from Bacillus. Moreover, it did not display the active site hepta-peptide motif RHGXRXP or the catalytically active dipeptide HD in acidic phytases. The mature protein of the PhyC had random coil (57.42%), extended strand (40.29%) and alpha helix (2.29%). The 3-D structure of the phyC was predicted by homologous modeling technology, the results indicated that the homology was 68.2% between the template protein (1h61 A) and the mature peptide of the phyC.
3. The construction of neutral phytase-producing engineered strains
The gene encoding B.licheniformis ZJ-6 neutral phytase (phyC) was cloned from vector pUCm-T phyCl by PCR. The phyC with original signal peptide was ligated into expression vector pET-30a(+) and transformed into Escherichia coli BL21 (DE3). The phyC was successfully expressed and the product, EPhyC5, was purified by Ni-NTA chromatography. The activity of purified EPhyC5 was 2.87U/mg. SDS-PAGE analysis showed that molecular mass of the purified EPhyC5 was 42.86kDa, which was similar to the the theory molecular mass,42.1 kDa.
The phyCm fragment encoding the mature peptide sequence of B.licheniformis ZJ-6 neutral phytase was amplified and cloned into expression vector pPIC9K. The pPIC9K-phyCm plasmid was linearized and transformed into Pichia Pastoris GS115 strain by electroporation. Positive strain was screened and purified by culturing on MD/MM plate and G418. After 96h 0.5% methanol induction, the activity of recombinant phytase (PPhyCm6) in culture supernatant of pPhyCm6 transformant was 8.64 U/mg. SDS-PAGE analysis showed that the molecular mass of PPhyCm6 was 38.78 kDa, which was in good agreement with the theory molecular mass, 38.7kDa.
4. Analyses of enzymatic properties of PhyC, EPhyC5 and PPhyCm6
The optimum temperature and pH of the PhyC were 55℃and 7.0, respectively. After treated at 80℃, pH 7.0 for 10 min, the residual activity of PhyC was 57.36%. Over 80% of PhyC activity was retained after treatment of the enzyme by preincubation over a pH range of 6.5-9.0 for 1 h at 25℃.
The optimum temperature and pH of the EPhyC5 were 60℃and 7.0, respectively. After treated at 80℃, pH 7.0 for 10 min, the residual activity of EPhyC5 was 68.26%. Over 80% of EPhyC5 activity was kept after treatment of the enzyme by preincubated over a pH range of 6.0-9.0 for 1 h at 25℃.
The optimum temperature and pH of the PPhyCm6 were 60℃and 7.5, respectively. After treated at 80℃, pH 7.5 for 10 min, the residual activity of PPhyCm6 was 59.42%. Over 80% of PPhyCm6 activity was retained after the enzyme treated by preincubation over a pH range of 5.0-9.0 for 1 h at 25℃.
The others enzymatic properties of the recombinant neutral phytase (EPhyC5 and PPhyCm6) were identical to those of the original enzyme. PhyC, EPhyC5 and PPhyCm6 were greatly inhibited by EDTA and metal ions such as Cd2+, Mn2+, Cu2+ and Ba2+. Their thermostabilities and pH stabilities could be improved in the presence of 1mmol/L Ca2+. All of them exhibit highly strict substrate specificity for sodium phytate and had no enzymatic activity on other phosphate esters tested. NaF and vanadate showed slight inhibition on their activities.
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