中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
Enhancement of alpha-cyclodextrin product specificity by enriching histidines of alpha-cyclodextrin glucanotransferase at remote subsite-6

文献类型:期刊论文

作者Yue, Yang1,2; Song, Binghong2; Xie, Ting2; Sun, Yan1; Chao, Yapeng2; Qian, Shijun2
刊名PROCESS BIOCHEMISTRY
出版日期2014-02-01
卷号49期号:2页码:230-236
关键词alpha-Cyclodextrin glucanotransferases alpha-Cyclodextrin Product specificity Site-directed mutagenesis Enzymatic properties
英文摘要The industrial use of a-cyclodextrins (alpha-CDs) has increased because their solubility is higher than those of beta-CDs. However, improving the product specificity of alpha-cyclodextrin glucanotransferases (CGTases) remains unresolved. In this study, three mutants (Y167-deletion, Y167HH, and Y167HHH) were constructed at subsite 6 of alpha-CGTase to investigate the contribution of amino acid residue 167 to the cyclization ability of alpha-CD by comparing it with Tyr167His mutant a-CGTase (previously constructed based on the wild-type gene of Bacillus sp. 602-1). As expected, the alpha:beta ratio improved with increasing number of histidine along with residue 167. The Y167HHH mutant had the highest alpha:beta ratio of 13.2 and almost produced single type a-CDs. The Y167HHH mutant enzyme was subsequently purified to homogeneity. The enzymatic properties and the optimal condition of Y167HHH mutant in converting raw starch were also investigated. This study discusses product specificity improvement by inserting specific amino acid residues in the active groove. The results indicate that the histidine-rich mutant alpha-CGTase possessed better potential in producing alpha-CDs in an industrial scale. (c) 2013 Published by Elsevier Ltd.
WOS标题词Science & Technology ; Life Sciences & Biomedicine ; Technology
类目[WOS]Biochemistry & Molecular Biology ; Biotechnology & Applied Microbiology ; Engineering, Chemical
研究领域[WOS]Biochemistry & Molecular Biology ; Biotechnology & Applied Microbiology ; Engineering
关键词[WOS]CIRCULANS STRAIN 251 ; SWISS-MODEL ; PROTEIN-STRUCTURE ; GLYCOSYLTRANSFERASE ; ENVIRONMENT ; INHIBITION ; MECHANISM ; BINDING ; ENZYME
收录类别SCI
语种英语
WOS记录号WOS:000332498200008
源URL[http://124.16.173.210/handle/834782/1408]  
专题天津工业生物技术研究所_酶工程实验室 马延和 _期刊论文
作者单位1.Beihang Univ BUAA, Key Lab Biomech & Mechanobiol, Minist Educ, Sch Biol Sci & Med Engn, Beijing 100191, Peoples R China
2.Chinese Acad Sci, Inst Microbiol, Natl Engn Lab Ind Enzymes, State Key Labs Transducer Technol, Beijing 100101, Peoples R China
推荐引用方式
GB/T 7714
Yue, Yang,Song, Binghong,Xie, Ting,et al. Enhancement of alpha-cyclodextrin product specificity by enriching histidines of alpha-cyclodextrin glucanotransferase at remote subsite-6[J]. PROCESS BIOCHEMISTRY,2014,49(2):230-236.
APA Yue, Yang,Song, Binghong,Xie, Ting,Sun, Yan,Chao, Yapeng,&Qian, Shijun.(2014).Enhancement of alpha-cyclodextrin product specificity by enriching histidines of alpha-cyclodextrin glucanotransferase at remote subsite-6.PROCESS BIOCHEMISTRY,49(2),230-236.
MLA Yue, Yang,et al."Enhancement of alpha-cyclodextrin product specificity by enriching histidines of alpha-cyclodextrin glucanotransferase at remote subsite-6".PROCESS BIOCHEMISTRY 49.2(2014):230-236.

入库方式: OAI收割

来源:天津工业生物技术研究所

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