Bioinformatics and molecular docking study of β-glucosidase J384W locus mutation
2024
PAN Hong | YAO Xiangyu | HONG Yinan | WANG Xiaojun | FAN Yurou
In order to improve the conversion efficiency of ginsenoside Rb1 by β-glucosidase, the key regions and sites involved in substrate recognition and binding in the conversion of ginsenoside Rb1 by β-glucosidase were obtained by molecular docking, the J384 site was fixed-point mutated to W384, and the physicochemical properties, hydrophilic/hydrophobicity, transmembrane region, and secondary/tertiary structure of the wild enzyme and the mutant enzyme were compared by bioinformatics. The results showed that altering the internal structure of the enzyme resulted in an increase in the number of binding sites and greater overall stability; and the mutant enzyme was more likely to spontaneously bind to ginsenoside Rb1 than the wild enzyme, with a minimum binding energy of -9.02 KJ/mol.
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