南海海洋微生物宏基因组文库中酯酶基因的筛选与鉴定
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摘要
自然环境中99%的微生物在目前的试验条件不易获得纯培养,极大限制了人类对微生物遗传资源的有效利用。现代生物科技以及严峻的能源危机对新型工业用酶的需求日益旺盛,极大的促进了新型开发环境遗传资源技术手段的发展。宏基因组学不依赖于微生物培养,提供了一个获取宝贵未培养微生物遗传资源的途径。在本研究中,采用宏基因组学的方法构建了一个高质量的南海海洋微生物宏基因组文库,通过高通量功能筛选,获得了五个酯酶阳性克隆,对其中两个具有较高活力的阳性克隆进行亚克隆,通过测序鉴定了酯酶的编码基因并分别命名为EstA和EstB,各自编码一个277和328个氨基酸的蛋白。氨基酸序列比对和分子进化树分析表明,EstA和在进化树上相近的可能具酯类水解活力蛋白形成一个家族,并与脂肪酶/酯酶FamilyⅢ相近,EstB和在进化树上相近的脂肪酶/酯酶形成了脂肪酶/酯酶FamilyⅣ的亚家族。定点突变试验表明EstA含有一个经典的催化三亚基结构(S146-D222-H255),而EstB含有一个不寻常的催化三亚基,由S149-E243-H273组成,这个特殊的催化三亚基构成这个亚家族的一个重要特征。异源表达纯化蛋白后,对EstA和EstB分别进行了酶学性质分析,结果表明EstA在多种阳离子中和高浓度的NaCl中表现出高度稳定性,反应了取样环境的高盐多离子的特征。EstB活力不受PMSF抑制,表明EstB可能具有一个类似于脂肪酶的lid结构。另外,EstB对对硝基苯酚酯类底物具有很高的催化活力,并且在30%的甲醇、乙醇、DMF、DMSO等有机溶剂中高度稳定,使得EstB成为一极具应用潜力的酯酶。
从环境中发掘重要的工业用酶用于工业应用,有利于节约原材料、节省能源,对于促进工业化发展和经济增长具有重要意义,同时也为开发海洋微生物的其它重要功能基因提供有力借鉴,为寻求海洋微生物资源最大限度挖掘、可持续开发利用的科学途径奠定理论基础。
99%of microbes in the environment cannot be cultured under laboratory conditions, which severely inhibited the full exploration of microbial genetic resources.The development of biotechnology and the criticality of energy crisis make the demand for novel biocatalysts is increasing in the morden world,which greatly stimulates the development of powerful tools to explore the genetic resources in the environment. Metagenomics,a culture independent strategy,provides an access to valuable genetic resources of the uncultured microbes.In this study,we have constructed a high quality metagenomic expression library from surface water microbes of South China Sea,five lipolytic active clones were isolated from this marine microbial metagenomic library by functional screening.Two novel esterase genes desinated as estA and estB,which encoded 277- and 328-amino-acid peptides respectively were discovered by subcloning and sequencing of two clones that displyed superior activity among them. Amino acid sequence comparison and phylogenetic analysis indicated that EstA together with other putative lipolytic enzymes was closely related to FamilyⅢ,and EstB with its relatives formed a subFamily of FamilyⅣ.Site-directed mutagenesis showed that EstA contained classical catalytic triad made up of S146-D222-H255, whereas EstB contained an unusual catalytic triad which consisted of S149-E243-H273,an important feature of the subFamily.Both of them were characterized after overexpressed and purified.EstA exhibited habitat-specific characteristics such as its high level of stability in the presence of various divalent cations and at high concentrations of NaCl.EstB was not inhibited by PMSF, suggested which may possesd a lipase-like lid structure.EstB displayed remarkable activity against p-nitrophenyl esters and was highly stable in 30%methanol,ethanol, dimethylformamide,and dimethyl sulfoxide,making EstB a potential candidate for industrial applications.
Mining important industrial enzymes from various environments is highly advantageous for industrial development and economic growth by reducing the energy and raw materials consumed in industrial process.In another aspect,it is also important in being a useful reference for exploration of other important functional genes from marine microbes and estabolishing a solid theoretical foundation for sustainable development and full utilization of marine microbial resources.
从环境中发掘重要的工业用酶用于工业应用,有利于节约原材料、节省能源,对于促进工业化发展和经济增长具有重要意义,同时也为开发海洋微生物的其它重要功能基因提供有力借鉴,为寻求海洋微生物资源最大限度挖掘、可持续开发利用的科学途径奠定理论基础。
99%of microbes in the environment cannot be cultured under laboratory conditions, which severely inhibited the full exploration of microbial genetic resources.The development of biotechnology and the criticality of energy crisis make the demand for novel biocatalysts is increasing in the morden world,which greatly stimulates the development of powerful tools to explore the genetic resources in the environment. Metagenomics,a culture independent strategy,provides an access to valuable genetic resources of the uncultured microbes.In this study,we have constructed a high quality metagenomic expression library from surface water microbes of South China Sea,five lipolytic active clones were isolated from this marine microbial metagenomic library by functional screening.Two novel esterase genes desinated as estA and estB,which encoded 277- and 328-amino-acid peptides respectively were discovered by subcloning and sequencing of two clones that displyed superior activity among them. Amino acid sequence comparison and phylogenetic analysis indicated that EstA together with other putative lipolytic enzymes was closely related to FamilyⅢ,and EstB with its relatives formed a subFamily of FamilyⅣ.Site-directed mutagenesis showed that EstA contained classical catalytic triad made up of S146-D222-H255, whereas EstB contained an unusual catalytic triad which consisted of S149-E243-H273,an important feature of the subFamily.Both of them were characterized after overexpressed and purified.EstA exhibited habitat-specific characteristics such as its high level of stability in the presence of various divalent cations and at high concentrations of NaCl.EstB was not inhibited by PMSF, suggested which may possesd a lipase-like lid structure.EstB displayed remarkable activity against p-nitrophenyl esters and was highly stable in 30%methanol,ethanol, dimethylformamide,and dimethyl sulfoxide,making EstB a potential candidate for industrial applications.
Mining important industrial enzymes from various environments is highly advantageous for industrial development and economic growth by reducing the energy and raw materials consumed in industrial process.In another aspect,it is also important in being a useful reference for exploration of other important functional genes from marine microbes and estabolishing a solid theoretical foundation for sustainable development and full utilization of marine microbial resources.
引文
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