Mutations in two amino acids in phyI1s from Aspergillus niger 113 improve its phytase activity
文献类型： 外文期刊
作者： Tian, Yong-Sheng 1 ; Peng, Ri-He 1 ; Xu, Jing 1 ; Zhao, Wei 1 ; Gao, Feng 1 ; Fu, Xiao-Yan 1 ; Xiong, Ai-Sheng 1 ; Yao, Q 1 ;
作者机构： 1.Shanghai Acad Agr Sci, Biotechnol Res Inst, Shanghai 201106, Peoples R China
关键词： enzyme kinetics;substrate binding;enzyme catalytic efficiency;enzyme structure-function study
期刊名称：WORLD JOURNAL OF MICROBIOLOGY & BIOTECHNOLOGY （ 影响因子：3.312； 五年影响因子：3.58 ）
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收录情况： SCI
摘要： We applied in vitro mutagenesis and colony screening, using the wild type phyI1s gene from Aspergillus niger 113 as the template, and obtained two mutant phyI1s (gene products) after one round of screening. The two mutants had mutations at two nucleic acid sites, resulting in changes in two amino acids: K41E, E121F. None of the amino acid substitutions in the two mutants was in a position reported to be important for catalysis or substrate binding. Kinetic analysis of the phytase activity of the two mutants indicated that the substitutions gave rise to 2.5- and 3.1-fold increased specific activity, and a 1.78- and 3.24-fold reduced affinity for sodium phytate. In addition, the overall catalytic efficiency (k (cat)/K (m)) of the two mutants was changed by 0.52-fold and 0.68-fold compared to that of the wild type. Such mutants will be instrumental for the structure-function study of the enzyme and for industrial application.
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