Comparative analysis of the white rot fungus Trametes hirsuta 072 laccases ability to modify 17β-oestradiol in the aqueous medium

IF 1.4 4区生物学 Q4 BIOCHEMISTRY & MOLECULAR BIOLOGY

Biocatalysis and Biotransformation Pub Date : 2022-06-13 DOI:10.1080/10242422.2022.2085034

O. Savinova, P. N. Solyev, T. Fedorova, S. Kochetkov, T. Savinova

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Abstract

Abstract A comparative study of the ability of Trametes hirsuta laccase isoenzymes to biotransform 17β-oestradiol (3,17β-dihydroxyestra-1,3,5(10)-triene, E2) was carried out. Native major LacA and recombinant minor isoenzymes (rLacC, rLacD, and rLacF) obtained in Penicillium canescens were used. It was found that all the studied isozymes are capable of catalysing the oxidative coupling of E2 in an aqueous medium (22 ± 2 °C, pH 4.5) with the formation of predominantly dimers and trimers. Other concurrently formed products were detected by high-pressure liquid chromatography – high-resolution mass spectrometry (HPLC–HRMS) and characterized, summarizing the overall condensation pathway of E2 in laccases. The highest catalytic activity was observed for major LacA. For other laccases, the activity decreased in the following sequence rLacF > rLacD > rLacC. Utilization of T. hirsuta enzymatic variety of laccases can be of benefit for detoxification of phenol-like steroid compounds in the environment.

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白腐菌毛毡菌072漆酶在水溶液中修饰17β-雌二醇能力的比较分析

摘要比较研究了毛毡菌漆酶同工酶转化17β-雌二醇(3,17β-二羟基雌二醇-1,3,5(10)-三烯，E2)的能力。本研究使用了从canescens青霉菌中获得的原生主要LacA酶和重组次要同工酶(rLacC、rLacD和rLacF)。结果表明，所研究的同工酶均能催化E2在22±2°C, pH 4.5的水溶液中氧化偶联，主要形成二聚体和三聚体。其他同时形成的产物通过高压液相色谱-高分辨率质谱(HPLC-HRMS)检测并表征，总结了E2在漆酶中的整体缩聚途径。主要LacA的催化活性最高。对于其他漆酶，活性降低的顺序为rLacF > rLacD > rLacC。利用毛霉酶类漆酶对环境中酚类甾类化合物的解毒具有重要意义。

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来源期刊

Biocatalysis and Biotransformation 生物-生化与分子生物学

CiteScore

4.40

自引率

5.60%

发文量

审稿时长

3 months

期刊介绍： Biocatalysis and Biotransformation publishes high quality research on the application of biological catalysts for the synthesis, interconversion or degradation of chemical species. Papers are published in the areas of: Mechanistic principles Kinetics and thermodynamics of biocatalytic processes Chemical or genetic modification of biocatalysts Developments in biocatalyst''s immobilization Activity and stability of biocatalysts in non-aqueous and multi-phasic environments, including the design of large scale biocatalytic processes Biomimetic systems Environmental applications of biocatalysis Metabolic engineering Types of articles published are; full-length original research articles, reviews, short communications on the application of biotransformations, and preliminary reports of novel catalytic activities.