Identification and characterization of Lacticaseibacillus rhamnosus HP-B1083-derived β-glucuronidase and its application for baicalin biotransformation
These videos have been matched automatically. Contact us if they are not relevant.
These videos have been matched automatically. Contact us if they are not relevant.
View abstract on PubMed
Summary
This summary is machine-generated.Lacticaseibacillus rhamnosus HP-B1083 produces a β-glucuronidase (GUS) enzyme, LrUidA, that efficiently converts baicalin to baicalein. This enzyme shows high activity and stability, enabling efficient industrial production of baicalein.
Area Of Science
- Biochemistry
- Enzymology
- Microbial Biotechnology
Background
- Baicalein possesses higher bioavailability and pharmacological activity than its precursor, baicalin.
- Baicalin can be transformed into baicalein via β-glucuronidase (GUS) catalysis.
- Lacticaseibacillus rhamnosus HP-B1083 has demonstrated efficient baicalin to baicalein biotransformation.
Purpose Of The Study
- To identify and characterize the GUS enzyme from L. rhamnosus HP-B1083 responsible for baicalin biotransformation.
- To elucidate the enzymatic properties and catalytic mechanism of the identified enzyme.
- To assess the enzyme's potential for industrial baicalein production.
Main Methods
- Cloning and sequencing of the LruidA gene encoding the GUS enzyme.
- Expression and purification of recombinant LrUidA enzyme.
- Enzyme characterization (optimal temperature, pH, kinetic parameters) and site-directed mutagenesis.
- Optimization of biotransformation reaction conditions.
Main Results
- The LruidA gene encodes a 70 kDa glycosyl hydrolase family 2 enzyme, LrUidA.
- LrUidA exhibits optimal activity at 50°C and pH 4.5, with good pH stability.
- Kinetic analysis revealed specific Michaelis-Menten, maximum velocity, and catalytic constant values.
- Mutagenesis identified key catalytic residues (E509, E415) and negatively charged residues (E450, D451, D452).
- Optimized conditions achieved a 99% conversion ratio of baicalin to baicalein within 4 hours.
Conclusions
- The characterized LrUidA enzyme from L. rhamnosus HP-B1083 is a highly efficient GUS for baicalin biotransformation.
- Understanding the enzyme's properties and catalytic mechanism facilitates its application in industrial baicalein production.
- This study expands knowledge on using GUS enzymes for the efficient synthesis of pharmacologically active compounds.
These videos have been matched automatically. Contact us if they are not relevant.
These videos have been matched automatically. Contact us if they are not relevant.