Enhancing Oxidative Stability of Glucose Oxidase from Aspergillus niger by Site-Directed Mutagenesis

doi:10.3969/j.issn.1673-1689.2016.12.005

Home > Archive>Volume 35, Issue 12, 2016 >1260-1267. DOI:10.3969/j.issn.1673-1689.2016.12.005

Enhancing Oxidative Stability of Glucose Oxidase from Aspergillus niger by Site-Directed Mutagenesis
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                        10.3969/j.issn.1673-1689.2016.12.005
                    
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Aiming to improve the catalytic activity and oxidative stability of glucose oxidase from Aspergillus niger. This work conducted site-directed mutagenesis based on an analysis of the protein structure. Four methionines（M582L，M524L，M556L and M305L） were selected as the mutation sites and individually replaced with leucine. The native GOD and the mutated GOD were separately expressed in P. pastoris GS115. In the presence of H2O2（10 mM，20 mM，50 mM，100 mM，and 500 mM） at 35 ℃ for 2 h，the oxidative stability of the mutants increased compared to the wild-type under most of the circumstances. Meanwhile，M556L showed a higher（2 folds than the wild-type） oxidative stability of all in the presence of both 100 mM and 500 mM H2O2 for 2 h. Compared to the wild-type enzyme，the kcat/Km value of M556L increased（2.08 folds than the wild-type）. The thermol stability of the mutants remained unchanged while the stable pH range of M524L was extended from 4.0-6.0 to 3.0-7.0 compared to the wild-type. It is a fact that a more stable enzyme with higher oxidative stability is an ideal choice in most of the industrial application of GOD.

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WEN Yifan, GU Lei, ZHANG Juan, DU Guocheng. Enhancing Oxidative Stability of Glucose Oxidase from Aspergillus niger by Site-Directed Mutagenesis[J]. Journal of Food Science and Biotechnology,2016,35(12):1260-1267.

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