@article{Jiang_Song_Xiao_Yang_Zhao_Gao_Liu_Liu_Xia_Li_Li_2016, title={Improving the anti-oxidation of glucose oxidase with computer-aided structure optimization}, volume={5}, url={https://rajpub.com/index.php/jbt/article/view/1483}, DOI={10.24297/jbt.v5i3.1483}, abstractNote={<p>Glucose oxidase (GOD) can be inactivated by hydrogen peroxide (H<sub>2</sub>O<sub>2</sub>) produced during glucose oxidation; thus, H<sub>2</sub>O<sub>2</sub> is a competitive inhibitor of GOD. In this mechanism, methionine (Met), a sulfur-containing amino acid, can be oxidized by H<sub>2</sub>O<sub>2</sub>and converted into methionine sulfoxide, thereby inactivating GOD. In this study, to block GOD oxidation, the two-dimensional structures of three mutants were designed with computer-aided analysis, and the complex structures of GOD mutants and their substrate glucose were determined using the CDOCKER algorithm. Three mutant GODs and the wild-type GOD were expressed in <em>Pichia pastoris</em>. After purification, the activities and anti-oxidation capacities were evaluated. The activity of GOD was decreased substantially from 3.24 U/μg in the wild-type protein to 0.05 U/μg in the GOD-M523L-M524L mutant; in contrast, the activity of GOD-M524L-M528L was not different from that of the wild-type protein. Because the activity of GOD-M523L-M524L was negligible, we did not evaluate its anti-oxidative effects. However, the mutant GOD-M524L-M528L had better anti-oxidation capacity than the wild-type GOD. These results were consistent with the results of computer-aided analysis, suggesting that this method may be useful for enzyme structure optimization.</p>}, number={3}, journal={JOURNAL OF ADVANCES IN BIOTECHNOLOGY}, author={Jiang, Zheng-Bing and Song, Hui-Ting and Xiao, Wen-Jing and Yang, Yi-Min and Zhao, Yong and Gao, Yuan and Liu, Shi-Hui and Liu, Zi-Lu and Xia, Wu-Cheng and Li, Rong and Li, Nuo-Nan}, year={2016}, month={May}, pages={736–740} }