Results: Recombinant glucose oxidase had 605 amino acids, with 29% α-helix, 16% β sheet and 54% coil in its secondary structure showing similarity to that of native glucose oxidase of A. The level of enzyme production was measured and analyzed by the software. Optimization of recombinant glucose oxidase for glucose, peptone, yeast extract and pH at four levels in YPD media with thiamine were defined to Qualitek-4 software. Materials & Methods: Protein sequence, primary, secondary and tertiary structures and glycosylation rate of recombinant glucose oxidase enzyme were studied via bioinformatics tools. The present study aimed to investigate bioinformatics characteristics of recombinant glucose oxidase in Yarrowia lipolytica Po1g-GOX and to optimize the production conditions of the enzyme by Taguchi experimental design method. Heterologous expression of the enzyme has been investigated in yeast hosts due to several industrial-scale limitations in enzyme production by Aspergillus niger. Background & Objectives: Glucose oxidase has a wide range of application in medical, pharmaceutical, food, textile, and environmental industries.
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