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作 者:戴斐[1] 张雍容[1] 江正兵[1] 魏东芝[1]
机构地区:[1]华东理工大学生物反应器工程国家重点实验室,上海200237
出 处:《华东理工大学学报(自然科学版)》2007年第2期177-180,204,共5页Journal of East China University of Science and Technology
摘 要:酿酒酵母表面展示脂肪酶重组菌株EBY100-pLHJ026在含半乳糖(20 g/L)的YNB-CAA培养基中进行诱导表达,脂肪酶在诱导48 h时酶活达到最高。以不同碳链长度的对硝基苯酚酯为底物对全细胞酶活进行性质检测,结果表明:对硝基苯酚癸酸酯(C10)为最适反应底物;全细胞脂肪酶在pH 8.0时的最适反应温度为37℃,在60℃保温2 h酶活保持90%,在60℃保温3 h酶活保持55%,表现出较好的热稳定性。在等体积二甲基亚砜中处理3 h后酶活保持28.4%。The lipase LipB52 displayed on the surface of the recombinant Saccharomy cescerevisiae strain EBY100-pLHJ026 was induced and expressed in YNB-CAA culture medium containing 20 g/L galactose. The enzyme activity reached the maximum after induced for 48 h. The whole cell enzyme activity was characterized with 4-nitrophenyl ramifications used as the substrate. Results show that the optimal substrate is 4-nitrophenylcaprate (C10). The optimal temperature for the whole cell lipase LipB52 was 37℃ at pH 8.0. After incubated for 2 h and 3 h at 60℃,90% and 55% of lipase activities remained respectively. The recombinant lipase displayed on cell surface exhibited favorable thermostability. The lipase remained 28.4% activity after incubated for 3 h in solvent containing 50% dimethyl sulfoxide.
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