[Improvement of catalytic activity and thermostability of glucose oxidase from

• DOI: 10.13345/j.cjb.240458
• Publication Date: 2025-01-25
• Authors: Shuxun Yu; Qiao Zhou; Honghai Zhang; Yingguo Bai; Huiying Luo; Xiaojun Yang; Bin Yao
• Keywords: Thermostability; Glucose oxidase

Glucose oxidase (GOD) is an oxygen-consuming dehydrogenase that can catalyze the production of gluconic acid hydrogen peroxide from glucose, and its specific mechanism action makes it promising for applications, while low catalytic activity poor thermostability have become main factors limiting industrial application this enzyme. In study, we used glucose AtGOD reported with best as source sequence phylogenetic analysis to obtain GOD excellent performance. Six genes were screened successfully synthesized functional validation. Among them, AhGODB derived Aspergillus heteromorphus was expressed in Pichia pastoris showed better activity, optimal temperature 40 ℃, a 112.2 U/mg, relative 47% after 5 min treatment at 70 ℃. To improve thermal stability, constructed several mutants by directed evolution combined rational design. Compared original enzyme, mutant T72R/A153P showcased optimum increasing 50 U/mg 166.1 ℃ 30 0% 33%. conclusion, obtained study improved thermostability, potential application.