Biotransformation of baicalin and glycyrrhizic acid using immobilized Fe₃O₄@Chitosan@β-glucuronidase.

ABSTRACT: β-Glucuronidase can hydrolyze β-glucuronic acid-containing glycosides, such as baicalin and glycyrrhizic acid. In this study, the β-glucuronidase gene from Lactobacillus rhamnosus was cloned and expressed in Escherichia coli. The resulting recombinant protein, designated LrhGUS, exhibited a molecular weight of approximately 72 kDa. The hydrolysis pathway of glycyrrhizic acid by recombinant LrhGUS proceeded as follows: glycyrrhizic acid → glycyrrhetinic acid monoglucuronide (GMAG) → glycyrrhetinic acid (GA), achieving a conversion rate of 90.38% with 2 mg/ml glycyrrhizic acid. Additionally, LrhGUS hydrolyzed baicalin into baicalein with a conversion rate of 94.64% using 20 mg/ml baicalin. Magnetic chitosan microspheres were utilized as carriers for immobilizing recombinant Lrh

SUBMITTER: Zhao Y 

PROVIDER: S-EPMC11829881 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature