| 解脂耶氏酵母脂肪酶Lip2的表面展示及其酶学性质 |
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| 引用本文： | 刘文山,赵鹤云,贾彬,徐莉,闫云君. 解脂耶氏酵母脂肪酶Lip2的表面展示及其酶学性质[J]. 微生物学通报, 2010, 37(2): 0174-0178 |
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| 作者姓名： | 刘文山 赵鹤云 贾彬 徐莉 闫云君 |
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| 作者单位： | 华中科技大学生命科学与技术学院,湖北武汉,430074 |
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| 基金项目： | 国家高技术研究与发展计划项目(No. 2006AA020203, 2007AA05Z417, 2007AA100703, 2009AA03Z232); 新世纪优秀人才支持计划(No. NCET-07-0336); 武汉市重点攻关计划(No. 200720422138) |
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| 摘 要： | 表面展示酶作为全细胞催化剂具备诸如能提高酶的稳定性、省去纯化过程、节约成本等优点。脂肪酶是应用最为广泛的工业酶之一。本研究利用酿酒酵母细胞壁蛋白Cwp2作为锚定蛋白,将解脂耶氏酵母脂肪酶Lip2展示在酿酒酵母细胞表面,以制备脂肪酶全细胞催化剂。Lip2被融合到Cwp2的N端,Cwp2通过其C端的GPI锚定信号共价结合到细胞壁上。表面展示的Lip2可以水解三丁酸甘油酯及对硝基苯酚辛酸酯(pNPC),其pNPC水解酶活达到4.6U/g干细胞。作为全细胞催化剂,表面展示的Lip2具备良好的催化特征,其最适温度为40°C,最适pH为8.0,同时还具备良好的有机溶剂稳定性。
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| 关 键 词： | 脂肪酶 解脂耶氏酵母 酿酒酵母 表面展示 全细胞催化剂 |
Cell Surface Display of Yarrowia lipolytica Lipase Lip2 by Saccharomyces cerevisiae and Its Practical Properties |
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| LIU Wen-Shan,ZHAO He-Yun,JIA Bin,XU Li and YAN Yun-Jun. Cell Surface Display of Yarrowia lipolytica Lipase Lip2 by Saccharomyces cerevisiae and Its Practical Properties[J]. Microbiology China, 2010, 37(2): 0174-0178 |
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| Authors: | LIU Wen-Shan ZHAO He-Yun JIA Bin XU Li YAN Yun-Jun |
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| Affiliation: | College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan, Hubei 430074, China;College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan, Hubei 430074, China;College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan, Hubei 430074, China;College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan, Hubei 430074, China;College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan, Hubei 430074, China |
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| Abstract: | Surface display of enzymes has been employed to improve stability of enzymes, and further save tedious purification process of enzymes to be used in conventional immobilization. Lipase is widely applied in industry. In this study, we constructed a Saccharomyces cerevisiae strain displaying lipase Lip2 from Yarrowia lipolytica on the cell surface. The gene encoding mature Lip2 was fused with the genes encoding the Kre1p leader sequence and the C-terminal domain of Cwp2 including the glycosylphosphatidylinositol(GPI)-anchor attachment signal. The Lip2 displayed on the yeast cell surface remained hydrolysis activity of lipase. The measured activity of the displayed lipase was 4.6 U/g dry cells. The displayed lipase was also characterized for its potentiality as a whole-cell biocatalyst. Its maximal activity was observed at 40°C and pH 8.0, and it exhibited good thermostability and high tolerance to organic solvent. |
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| Keywords: | Lipase Yarrowia lipolytica Saccharomyces cerevisia Surface display Whole-cell biocatalyst |
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