Heterologous expression of a novel β-glucosidase BglD2 and its application in polydatin-hydrolyzing.
- Author:
Cheng HE
1
;
Yan WU
1
;
Chunyu MENG
1
;
Yazhong XIAO
1
;
Zemin FANG
1
;
Wei FANG
1
Author Information
- Publication Type:Journal Article
- Keywords: ethanol tolerance; glucose tolerance; polydatin; resveratrol; β-glucosidase
- MeSH: Enzyme Stability; Glucose; Glucosides/pharmacology*; Hydrogen-Ion Concentration; Stilbenes/pharmacology*; Substrate Specificity; Temperature; Xylose; beta-Glucosidase/genetics*
- From: Chinese Journal of Biotechnology 2021;37(2):580-592
- CountryChina
- Language:Chinese
- Abstract: A novel β-glucosidase BglD2 with glucose and ethanol tolerant properties was screened and cloned from the deep-sea bacterium Bacillus sp. D1. The application potential of BglD2 toward polydatin-hydrolyzing was also evaluated. BglD2 exhibited the maximal β-glucosidase activity at 45 °C and pH 6.5. BglD2 maintained approximately 50% of its origin activity after incubation at 30 °C and pH 6.5 for 20 h. BglD2 could hydrolyze a variety of substrates containing β (1→3), β (1→4), and β (1→6) bonds. The activity of β-glucosidase was enhanced to 2.0 fold and 2.3 fold by 100 mmol/L glucose and 150 mmol/L xylose, respectively. BglD2 possessed ethanol-stimulated and -tolerant properties. At 30 °C, the activity of BglD2 enhanced to 1.2 fold in the presence of 10% ethanol and even remained 60% in 25% ethanol. BglD2 could hydrolyze polydatin to produce resveratrol. At 35 °C, BglD2 hydrolyzed 86% polydatin after incubation for 2 h. Thus, BglD2 possessed glucose and ethanol tolerant properties and can be used as the potential candidate of catalyst for the production of resveratrol from polydatin.
