Enzymatic biotransformation of ginsenoside Rb1 to compound K by recombinant β-glucosidase from Microbacterium esteraromaticum.

@article{Quan2012EnzymaticBO,
  title={Enzymatic biotransformation of ginsenoside Rb1 to compound K by recombinant β-glucosidase from Microbacterium esteraromaticum.},
  author={Lin-Hu Quan and Jin-Woo Min and Yan Jin and Chao Wang and Yeon-Ju Kim and Deok-Chun Yang},
  journal={Journal of agricultural and food chemistry},
  year={2012},
  volume={60 14},
  pages={3776-81}
}
We cloned and characterized a β-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… CONTINUE READING