Enzymatic biotransformation of ginsenoside Rb1 to compound K by recombinant ß-glucosidase from Microbacterium esteraromaticum.
J Agric Food Chem
; 60(14): 3776-81, 2012 Apr 11.
Article
in En
| MEDLINE
| ID: mdl-22428991
ABSTRACT
We cloned and characterized a ß-glucosidase (bgp3) gene from Microbacterium esteraromaticum isolated from ginseng field. The bgp3 gene consists of 2,271 bp encoding 756 amino acids which have homology to the glycosyl hydrolase family 3 protein domain. The molecular mass of purified Bgp3 was 80 kDa, as determined by SDS-PAGE. The enzyme (Bgp3) catalyzed the conversion of ginsenoside Rb1 to the more pharmacologically active minor ginsenoside Rd and compound K. The Bgp3 hydrolyzed the outer glucose moiety attached to the C-20 position of ginsenoside Rb1, followed by hydrolysis of the inner glucose moiety attached to the C-3 position. Using 0.1 mg mL(-1) enzyme in 20 mM sodium phosphate buffer at 40 °C and pH 7.0, 1.0 mg mL(-1) ginsenoside Rb1 was transformed into 0.46 mg mL(-1) compound K within 60 min with a corresponding molar conversion yield of 77%. Bgp3 hydrolyzed the ginsenoside Rb1 along the following pathway Rb1 â Rd â compound K.
Full text:
1
Database:
MEDLINE
Main subject:
Actinomycetales
/
Beta-Glucosidase
/
Ginsenosides
Language:
En
Year:
2012
Type:
Article