O. Savinova, P. N. Solyev, T. Fedorova, S. Kochetkov, T. Savinova
{"title":"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","authors":"O. Savinova, P. N. Solyev, T. Fedorova, S. Kochetkov, T. Savinova","doi":"10.1080/10242422.2022.2085034","DOIUrl":null,"url":null,"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.","PeriodicalId":8824,"journal":{"name":"Biocatalysis and Biotransformation","volume":"41 1","pages":"475 - 485"},"PeriodicalIF":1.4000,"publicationDate":"2022-06-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Comparative analysis of the white rot fungus Trametes hirsuta 072 laccases ability to modify 17β-oestradiol in the aqueous medium\",\"authors\":\"O. Savinova, P. N. Solyev, T. Fedorova, S. Kochetkov, T. Savinova\",\"doi\":\"10.1080/10242422.2022.2085034\",\"DOIUrl\":null,\"url\":null,\"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.\",\"PeriodicalId\":8824,\"journal\":{\"name\":\"Biocatalysis and Biotransformation\",\"volume\":\"41 1\",\"pages\":\"475 - 485\"},\"PeriodicalIF\":1.4000,\"publicationDate\":\"2022-06-13\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biocatalysis and Biotransformation\",\"FirstCategoryId\":\"5\",\"ListUrlMain\":\"https://doi.org/10.1080/10242422.2022.2085034\",\"RegionNum\":4,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q4\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biocatalysis and Biotransformation","FirstCategoryId":"5","ListUrlMain":"https://doi.org/10.1080/10242422.2022.2085034","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
Comparative analysis of the white rot fungus Trametes hirsuta 072 laccases ability to modify 17β-oestradiol in the aqueous medium
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.
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.