Bioinformatics and molecular docking study of β-glucosidase J384W locus mutation
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 ginsen-oside Rb1 by β-glucosidase were obtained by molecular docking,the J384 site was fixed-point mu-tated to W384,and the physicochemical properties,hydrophilic/hydrophobicity,transmembrane region,and secondary/tertiary structure of the wild enzyme and the mutant enzyme were com-pared by bioinformatics.The results showed that altering the internal structure of the enzyme re-sulted 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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