Enhancement of α-cyclodextrin product specificity by enriching histidines of α-cyclodextrin glucanotransferase at remote subsite −6
作者： Yang Yue , Binghong Song , Ting Xie , Yan Sun , Yapeng Chao
DOI: 10.1016/J.PROCBIO.2013.11.002
关键词: Cyclodextrin 、 Starch 、 Site-directed mutagenesis 、 Solubility 、 Enzyme 、 Biochemistry 、 Histidine 、 Residue (chemistry) 、 Mutant 、 Chemistry 、 Stereochemistry
摘要: Abstract The industrial use of α-cyclodextrins (α-CDs) has increased because their solubility is higher than those β-CDs. However, improving the product specificity α-cyclodextrin glucanotransferases (CGTases) remains unresolved. In this study, three mutants (Y167-deletion, Y167HH, and Y167HHH) were constructed at subsite −6 α-CGTase to investigate contribution amino acid residue 167 cyclization ability α-CD by comparing it with Tyr167His mutant (previously based on wild-type gene Bacillus sp. 602-1). As expected, α:β ratio improved increasing number histidine along 167. Y167HHH had highest 13.2 almost produced single type α-CDs. enzyme was subsequently purified homogeneity. enzymatic properties optimal condition in converting raw starch also investigated. This study discusses improvement inserting specific residues active groove. results indicate that histidine-rich possessed better potential producing α-CDs an scale.
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