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Complete Biotransformation of Protopanaxadiol-Type Ginsenosides into 20-O-ß-Glucopyranosyl-20(S)-protopanaxadiol by Permeabilized Recombinant Escherichia coli Cells Coexpressing ß-Glucosidase and Chaperone Genes.
Kim, Se-A; Shin, Kyung-Chul; Oh, Deok-Kun.
Afiliação
  • Kim SA; Department of Bioscience and Biotechnology , Konkuk University , Seoul 05029 , Republic of Korea.
  • Shin KC; Department of Bioscience and Biotechnology , Konkuk University , Seoul 05029 , Republic of Korea.
  • Oh DK; Department of Bioscience and Biotechnology , Konkuk University , Seoul 05029 , Republic of Korea.
J Agric Food Chem ; 67(30): 8393-8401, 2019 Jul 31.
Article em En | MEDLINE | ID: mdl-31291721
ABSTRACT
The ginsenoside 20-O-ß-glucopyranosyl-20(S)-protopanaxadiol or compound K is an essential ingredient in functional food, cosmetics, and traditional medicines. However, no study has reported the complete conversion of all protopanaxadiol (PPD)-type ginsenosides from ginseng extract into compound K using whole-cell conversion. To increase the production of compound K from ginseng extract using whole recombinant cells, the ß-glucosidase enzyme from Caldicellulosiruptor bescii was coexpressed with a chaperone expression system (pGro7), and the cells expressing the coexpression system were permeabilized with ethylenediaminetetraacetic acid. The permeabilized cells carrying the chaperone coexpression system showed a 2.6-fold increase in productivity and yield as compared with nontreated cells, and completely converted all PPD-type ginsenosides from ginseng root extract into compound K with the highest productivity among the results reported so far. Our results will contribute to the industrial biological production of compound K.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Sapogeninas / Proteínas de Bactérias / Beta-Glucosidase / Chaperonas Moleculares / Ginsenosídeos / Escherichia coli / Firmicutes Idioma: En Ano de publicação: 2019 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Sapogeninas / Proteínas de Bactérias / Beta-Glucosidase / Chaperonas Moleculares / Ginsenosídeos / Escherichia coli / Firmicutes Idioma: En Ano de publicação: 2019 Tipo de documento: Article