Mechanistic study for catalytic promiscuity of phenylalanine dehydrogenase induced by amino acid deep eutectic solvents

IF 4 3区工程技术 Q2 ENGINEERING, CHEMICAL

AIChE Journal Pub Date : 2025-07-02 DOI:10.1002/aic.18937

Yuxin Chen, Qian Zhang, Shizhen Wang

引用次数: 0

Abstract

Catalytic promiscuity of phenylalanine dehydrogenase (NTAaDH) induced by the amino acid deep eutectic solvents (AA‐DES) was studied. The activity of NTAaDH with the L‐Phe‐DES as substrate was 71.7‐fold that of the buffer system, while it was 24.4‐fold for L‐Lys‐DES. The half‐life of NTAaDH was enhanced by threefold of that of buffer at 50°C. Mechanism of catalytic promiscuity induced by AA‐DES was studied. AA‐DES can biomimetic intracellular environment with a crowding effect and provide a protective layer of enzyme. Analysis of the conformation change of NTAaDH indicated the shrinkage of the substrate channel. This study provided a new strategy for the solvent engineering for the oxidoreductases and further for industrial production.

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氨基酸深度共熔溶剂诱导苯丙氨酸脱氢酶催化混杂的机理研究

研究了氨基酸深度共熔溶剂（AA‐DES）对苯丙氨酸脱氢酶（NTAaDH）的催化乱交性。以L‐Phe‐DES为底物的NTAaDH活性是缓冲体系的71.7倍，以L‐Lys‐DES为底物的NTAaDH活性是缓冲体系的24.4倍。在50℃时，NTAaDH的半衰期是缓冲液的3倍。研究了AA‐DES催化乱交的机理。AA‐DES可以模拟细胞内环境，具有拥挤效应，并提供酶的保护层。分析NTAaDH的构象变化表明衬底通道收缩。本研究为氧化还原酶的溶剂工程及工业化生产提供了新的思路。

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

AIChE Journal 工程技术-工程：化工

CiteScore

7.10

自引率

10.80%

发文量

411

审稿时长

3.6 months

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