Abstract

Resveratrol, an ingredient of traditional Chinese medicine, has beneficial effects on human health and huge potential for application in modern medicine. Polydatin is extracted from plants and then deglycosylated into resveratrol; enzymatic methods are preferred for this reaction. In this study, a β-D-glucosidase from Sphingomonas showed high efficiency in transforming polydatin into resveratrol and was tolerant toward organic solvents. Applying this enzyme in a biphasic transformation system resulted in 95.3% conversion of 20% concentration crude polydatin to resveratrol in 4 h. We thus report a new method for high-efficiency, clean production of resveratrol.

Highlights

  • Compared with resveratrol synthesized by chemical synthesis, resveratrol produced by the P. cuspidatum extraction process is more economical and has been widely used

  • [17].The poor aqueous solubility and good organic solvent solubility of polydatin and resveratrol result in another complication in both enzymatic whole-cell conversions

  • At 60 °C, only 10.07% of the polydatin was transformed into resveratrol (Figure 6B)

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Summary

Introduction

Aspergillus showed preferable characteristics and high high overall conversion efficiency in converting to resveratrol. [17].The poor aqueous solubility and good organic solvent solubility of polydatin and resveratrol result in another complication in both enzymatic whole-cell conversions. Theare substrate theaqueous productsolutions are mixed andlittle precipitated, Generally, conversion reactions carried and out in with or no orand the product must be recovered using organic solvent extraction [19]. Toup overcome the conversion problem of resveratrol, a biphase transformation sysThis preferable characteristics in converting polydatin resveratrol and tem enzyme was setshowed up using a β-D-glucosidase, named. This enzyme showed preferable characteristics in converting polydatin to resulted in good polydatin to resveratrol and high This product purity. Biphase biotransformation system resulted in good conversion of polydatin to resveratrol and high product

Results
SDS polyacrylamide gelgel electrophoresis analysis of of purified recombinant
Optimal
Comparison of Uniaphase
Conversion
Optimization of Biphase Enzymatic Conversion System
Discussion
Bacterial Strains and Growth Conditions
Cloning of SpBGL1
Heterologous Expression of SpBGL1
Enzyme Activity Assays
Enzymatic Characterization of SpBGL1
Optimal Enzymatic Conditions for Catalysis of Polydatin by SpBGL1
Enzymatic Hydrolysis Assay in The Uniphase and Biphasic Conversion Systems
Conclusions
Full Text
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