Spectroscopic and in silico investigation of the interaction between GH1 β-glucosidase and ginsenoside Rb₁.

ABSTRACT: The function and application of β-glucosidase attract attention nowadays. β-glucosidase was confirmed of transforming ginsenoside Rb₁ to rare ginsenoside, but the interaction mechanism remains not clear. In this work, β-glucosidase from GH1 family of Paenibacillus polymyxa was selected, and its gene sequence bglB was synthesized by codon. Then, recombinant plasmid was transferred into Escherichia coli BL21 (DE3) and expressed. The UV-visible spectrum showed that ginsenoside Rb₁ decreased the polarity of the corresponding structure of hydrophobic aromatic amino acids (Trp) in β-glucosidase and increased new π-π^* transition. The fluorescence quenching spectrum showed that ginsenoside Rb₁ inhibited intrinsic fluorescence, formed

SUBMITTER: Zhong S 

PROVIDER: S-EPMC8020931 | biostudies-literature | 2021 Apr

REPOSITORIES: biostudies-literature