Remodeling the Active Site of Sucrose Phosphorylase for Effective Resveratrol Glycosylation.

IF 3.9 2区生物学 Q2 BIOTECHNOLOGY & APPLIED MICROBIOLOGY

Biotechnology and Bioengineering Pub Date : 2026-09-27 DOI:10.1002/bit.70383

Changxin Lu, Xin Wang, Shuaibin Du, Jiajia He, Hanchi Chen, Linjiang Zhu, Xiaolong Chen

引用次数: 0

Abstract

The plasticity of the enzyme active site is widespread in naturally evolved homologous enzymes, but has been less explored in engineered enzymes. In this study, the plasticity of the active site in sucrose phosphorylases (SPs) for 3-O-α-glucopyranosyl-resveratrol synthesis was obtained. The mutant R135L/Y344Q of BlSP from Bifidobacterium lactis showed the same catalytic activity with the previous mutant Q345F, but displayed different microenvironment of active site and enzymatic properties. The new mutant could almost completely convert up to 15 g/L resveratrol into resveratrol glycoside without cosolvent, meanwhile, generate a new impurity 3-O-α-diglucoside-resveratrol, which was identified as 3-O-α-maltosyl-resveratrol.

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蔗糖磷酸化酶活性位点的重塑促进白藜芦醇有效糖基化。

酶活性位点的可塑性在自然进化的同源酶中广泛存在，但在工程酶中研究较少。在本研究中，获得了蔗糖磷酸化酶（SPs）合成3-O-α-glucopyranosyl-resveratrol活性位点的可塑性。来自乳酸双歧杆菌的BlSP突变体R135L/Y344Q与之前的突变体Q345F具有相同的催化活性，但表现出不同的微环境活性位点和酶性质。该突变体在无助溶剂的情况下可将高达15 g/L的白藜芦醇几乎完全转化为白藜芦醇苷，同时生成新的杂质3-O-α-二葡糖苷-白藜芦醇，经鉴定为3-O-α-麦芽糖基-白藜芦醇。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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来源期刊

Biotechnology and Bioengineering 工程技术-生物工程与应用微生物

CiteScore

7.90

自引率

5.30%

发文量

280

审稿时长

2.1 months

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