Heterologous expression of a novel β-glucosidase BglD2 and its application in polydatin-hydrolyzing / 生物工程学报
Chinese Journal of Biotechnology
;
(12): 580-592, 2021.
Article
in Chinese
| WPRIM
| ID: wpr-878583
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.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Stilbenes
/
Substrate Specificity
/
Temperature
/
Xylose
/
Enzyme Stability
/
Beta-Glucosidase
/
Glucose
/
Glucosides
/
Hydrogen-Ion Concentration
Language:
Chinese
Journal:
Chinese Journal of Biotechnology
Year:
2021
Type:
Article
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