Identification of β-Glucosidase Activity of Lentilactobacillus buchneri URN103L and Its Potential to Convert Ginsenoside Rb1 from Panax ginseng

• Published in: Foods 2022-02, Vol.11 (4), p.529
• Main Authors: Renchinkhand, Gereltuya, Magsar, Urgamal, Bae, Hyoung Churl, Choi, Suk-Ho, Nam, Myoung Soo
• Format: Article
• Language: English
• Subjects: Bacteria; Chromatography; Cosmetics; Enzymes; Esculin; Fermentation; Fermented food; Food; Food plants; Food science; Functional foods & nutraceuticals; Ginseng; ginsenoside Rb1; Ginsenosides; Glucosidase; Homology; hydrolyze; Lactic acid; Lactic acid bacteria; Legumes; Lentilactobacillus buchneri URN103L; Leucine; Metabolites; Panax ginseng; Probiotics; Rg3; Valine; Variance analysis; β-Glucosidase
• ISSN: 2304-8158; 2304-8158
• DOI: 10.3390/foods11040529

isolated from Korean fermented plant foods produces β-glucosidase, which can hydrolyze ginsenoside Rb1 from Panax ginseng to yield ginsenoside Rd. The aim of this study was to determine the mechanisms underlying the extracellular β-glucosidase activity obtained from URN103L. Among the 17 types of lactic acid bacteria showing positive β-glucosidase activity in the esculin iron agar test, only URN103L was found to exhibit high hydrolytic activity on ginsenoside Rb1. The strain showed 99% homology with NRRLB 30929, whereby it was named URN103L. Supernatants of selected cultures with β-glucosidase activity were examined for hydrolysis of the major ginsenoside Rb1 at 40 °C, pH 5.0. Furthermore, the β-glucosidase activity of this strain showed a distinct ability to hydrolyze major ginsenoside Rb1 into minor ginsenosides Rd and Rg3. URN103L showed higher leucine arylamidase, valine arylamidase, α-galactosidass, β-galactosidase, and β-glucosidase activities than any other strain. We conclude that β-glucosidase from URN103L can effectively hydrolyze ginsenoside Rb1 into Rd and Rg3. The converted ginsenoside can be used in functional foods, yogurts, beverage products, cosmetics, and other health products.