A highly versatile fungal glucosyltransferase for specific production of quercetin-7-O-β-d-glucoside and quercetin-3-O-β-d-glucoside in different hosts

槲皮素 生物化学 毕赤酵母 葡萄糖苷 葡萄糖基转移酶 大肠杆菌 恶臭假单胞菌 生物 化学 重组DNA 医学 替代医学 病理 基因 抗氧化剂
作者
Jie Ren,Wenzhu Tang,Caleb Don Barton,Owen M. Price,Mark Wayne Mortensen,Alexandra Phillips,B. Wald,Simon Elgin Hulme,Logan Powell Stanley,Joan M. Hevel,Jixun Zhan
出处
期刊:Applied Microbiology and Biotechnology [Springer Science+Business Media]
卷期号:106 (1): 227-245 被引量:17
标识
DOI:10.1007/s00253-021-11716-x
摘要

Glycosylation is an effective way to improve the water solubility of natural products. In this work, a novel glycosyltransferase gene (BbGT) was discovered from Beauveria bassiana ATCC 7159 and heterologously expressed in Escherichia coli. The purified enzyme was functionally characterized through in vitro enzymatic reactions as a UDP-glucosyltransferase, converting quercetin to five monoglucosylated and one diglucosylated products. The optimal pH and temperature for BbGT are 35 ℃ and 8.0, respectively. The activity of BbGT was stimulated by Ca2+, Mg2+, and Mn2+, but inhibited by Zn2+. BbGT enzyme is flexible and can glycosylate a variety of substrates such as curcumin, resveratrol, and zearalenone. The enzyme was also expressed in other microbial hosts including Saccharomyces cerevisiae, Pseudomonas putida, and Pichia pastoris. Interestingly, the major glycosylation product of quercetin in E. coli, P. putida, and P. pastoris was quercetin-7-O-β-D-glucoside, while the enzyme dominantly produced quercetin-3-O-β-D-glucoside in S. cerevisiae. The BbGT-harboring E. coli and S. cerevisiae strains were used as whole-cell biocatalysts to specifically produce the two valuable quercetin glucosides, respectively. The titer of quercetin-7-O-β-D-glucosides was 0.34 ± 0.02 mM from 0.83 mM quercetin in 24 h by BbGT-harboring E. coli. The yield of quercetin-3-O-β-D-glucoside was 0.22 ± 0.02 mM from 0.41 mM quercetin in 12 h by BbGT-harboring S. cerevisiae. This work thus provides an efficient way to produce two valuable quercetin glucosides through the expression of a versatile glucosyltransferase in different hosts. KEY POINTS: • A highly versatile glucosyltransferase was identified from B. bassiana ATCC 7159. • BbGT converts quercetin to five mono- and one di-glucosylated derivatives in vitro. • Different quercetin glucosides were produced by BbGT in E. coli and S. cerevisiae.
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