Site-saturation mutagenesis of proline 176 in Cyclodextrin Glucosyltransferase from Bacillus sp. Y112 effects product specificity and enzymatic properties
文献类型： 外文期刊
作者： Li, Xiaohan 2 ; Sun, Jingjing 1 ; Wang, Wei 1 ; Guo, Jiaomei 2 ; Song, Kai 2 ; Hao, Jianhua 1 ;
作者机构： 1.Chinese Acad Fishery Sci, Yellow Sea Fisheries Res Inst, Key Lab Sustainable Dev Polar Fishery, Minist Agr & Rural Affairs, Qingdao 266071, Peoples R China
2.Shanghai Ocean Univ, Coll Food Sci & Technol, Shanghai 201306, Peoples R China
3.Qingdao Natl Lab Marine Sci & Technol, Lab Marine Drugs & Bioprod, Qingdao 266071, Peoples R China
4.Jiangsu Collaborat Innovat Ctr Exploitat & Utiliz, Lianyungang 222005, Peoples R China
关键词： Cyclodextrin glycosyltransferases; Site-saturation mutagenesis; Site Pro176; Cyclodextrin; Product specificity
期刊名称：PROCESS BIOCHEMISTRY （ 影响因子：3.757； 五年影响因子：3.665 ）
ISSN： 1359-5113
年卷期： 2020 年 94 卷
页码：
收录情况： SCI
摘要： Based on the analysis of amino acid sequence and simulated structure, saturation mutagenesis was performed to explore the role of the site p176 of cyclodextrin glucosytransferase (CGTase) from Bacillus sp. Y112. Compared to the wild-type, mutant P176G showed 10.4 % improvement in conversion from starch to cyclodextrins (CDs), whose beta-CD yield increased by 6% and alpha-CD yield decreased by 8%. Mutants P176L and P176I were increased by 7.9 % and 9.4 % on CDs production, indicating replacement of hydrophobic amino acids significantly improved in cyclization activity. Kinetics studies indicated the substrate affinity of P176G and P176K were increase by 13 % and 14 %, and the catalytic efficiency of P176K was increase by 14 %. In addition, the optimal temperature of mutants transformed from 50 degrees C to 40 degrees C and the optimal pH shifted from 10.0 to 8.0. These results indicate that the site P176 plays a critical role in catalytic activity, product specificity and enzymatic properties of CGTase.
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