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微生物来源α-L-鼠李糖苷酶的分子和结构生物学研究进展

Progresses on Molecular Biology and Structural Biology of α-L-rhamnosidase from Microbial Sources

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【作者】 张霞李利君倪辉蔡慧农苏文金

【Author】 ZHANG Xia;LI Li-jun;NI Hui;CAI Hui-nong;SU Wen-jin;College of Bioengineering, Jimei University;Research Center of Food Microbiology and Enzyme Engineering Technology;Research Center of Food Biotechnology of Xiamen City;

【机构】 集美大学生物工程学院福建省高校食品微生物与酶工程技术研究中心厦门市食品与生物工程技术研究中心

【摘要】 α-L-鼠李糖苷酶(α-L-rhamnosidase(EC 3.2.1.40))是一种水解酶,分布在GH13、GH28、GH78和GH106家族,其中3种GH78家族的α-L-鼠李糖苷酶具有典型的(α/α)6桶状结构,它能够特异性地水解许多糖苷类物质末端的α-L-鼠李糖基,在食品饮料加工工业和医药业中具有重要的应用价值。介绍了微生物来源的α-L-鼠李糖苷酶的性质及应用,主要阐述了α-L-鼠李糖苷酶基因的克隆、表达及该酶晶体结构方面的研究进展。

【Abstract】 α-L-rhamnosidase(EC 3.2.1.40) cleaves terminal α-L-rhamnose specifically from a large number of glycosides. The enzyme is a biotechnologically important hydrolytic enzyme due to its applications in the food and beverage processing industry and pharmaceutical industry. Based on primary sequence similarities, α-L-rhamnosidases are classified within the Carbohydrate-active enzymes(CAZy) database into four glycoside hydrolase(GH) families(GH13, GH28, GH78 and GH106 family), and three α-L-rhamnosidases of GH78 have a typical(α/α)6-barrel structure. Properties and applications of α-L-rhamnosidase from different microbial sources have been introduced. In addition, the recent developments on cloning, expression of α-L-rhamnosidase gene and the crystal structure of the enzyme were summarized.

【基金】 国家自然科学基金项目(31371751);福建省自然科学基金项目(2011J01225)
  • 【文献出处】 生命科学研究 ,Life Science Research , 编辑部邮箱 ,2015年01期
  • 【分类号】Q55
  • 【被引频次】14
  • 【下载频次】773
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