| Bispora sp. MEY-1来源的嗜酸海藻糖酶TreA酶学性质研究 |
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| 引用本文： | 蒋肖,涂涛,王坤,彤丽格,罗会颖.Bispora sp. MEY-1来源的嗜酸海藻糖酶TreA酶学性质研究[J].中国农业科技导报,2021,23(4):85-92. |
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| 作者姓名： | 蒋肖 涂涛 王坤 彤丽格 罗会颖 |
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| 作者单位： | 中国农业科学院饲料研究所, 农业农村部饲料生物技术重点实验室, 北京 100081 |
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| 基金项目： | 现代农业产业技术体系项目（CARS-41） |
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| 摘 要： | 酸性海藻糖酶作为生物催化剂在生物工业中广泛应用，挖掘酶学性质优良的酸性海藻糖基因具有重要意义。从Bispora sp. MEY-1中成功克隆出一个酸性海藻糖酶基因TreA，并在毕赤酵母GS115中实现高效表达。对纯化后的酸性海藻糖酶TreA进行酶学性质鉴定，其最适pH为4.0，在pH 2.2~5.0范围内，该酶能够维持60%以上的酶活力。TreA在偏酸条件下稳定效果比较好，在pH 1.0~4.0条件下处理1 h，可以剩余88%以上的酶活力。TreA的最适温度为60 ℃，在40~70 ℃之间都可以维持50%以上的酶活力，属于中高温酶。重组海藻糖酶TreA的比活为1 913 U·mg-1，动力学参数Km和Vmax分别为0.67 mg·mL-1和119 μmol·min-1·mg-1。同时，还评估了不同金属离子或化学试剂对纯海藻糖酶TreA的酶活性影响及其蛋白酶抗性。极大丰富了海藻糖酶基因资源，促进了其在生物工业中的应用。
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| 关 键 词： | Bispora sp. MEY-1 酸性海藻糖酶 异源表达 酶学性质鉴定 |
| 收稿时间： | 2020-05-25 |
Enzymatic Properties of an Acidic Trehalase TreA from Bispora sp. MEY-1#br# |
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| JIANG Xiao,TU Tao,WANG Kun,TONG Lige,LUO Huiying.Enzymatic Properties of an Acidic Trehalase TreA from Bispora sp. MEY-1#br#[J].Journal of Agricultural Science and Technology,2021,23(4):85-92. |
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| Authors: | JIANG Xiao TU Tao WANG Kun TONG Lige LUO Huiying |
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| Institution: | Key Laboratory for Feed Biotechnology, Ministry of Agriculture and Rural Affairs; Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China |
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| Abstract: | As a biocatalystase, acid trehalase is widely used in biological industry. It is very important to exploit new acid trehalase with excellent enzymatic properties. In this study, an acid trehalase gene (TreA) from Bispora sp. MEY-1 was successfully cloned and expressed in Pichia pastoris GS115. The enzymatic properties of purified trehalase TreA were identified. The optimum pH was 4.0, and the relative activity maintained over 60% under the range of pH 2.2~5.0. The relative activity of purified enzyme was more than 88% after treated for 1 h under pH 1.0~4.0, which exhibited the good acid stability. The optimum temperature of purified enzyme was 60 ℃, which was enzyme with medium-high temperature resistance. The specific activity of purified enzyme was 1 913 U·mg-1, and its Km and Vmax were 0.67 mg·mL-1 and 119 μmol·min-1·mg-1, respectively. Moreover, the effects of different mental ions or chemical reagents, and the protease resistances on the purified enzyme activity were also evaluated. |
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| Keywords: | Bispora sp MEY-1 acid trehalase heterologous expression characterization |
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