{"title":"Peroxidase of Trametes hirsuta LE-BIN 072: Purification, Characteristics, and Application for Dye Decolorization","authors":"O. S. Savinova, T. V. Fedorova","doi":"10.1134/S0003683824605730","DOIUrl":null,"url":null,"abstract":"<p>Lignin peroxidase (<b>LiP9</b>) from the basidiomycete <i>Trametes hirsuta</i> LE-BIN 072, an effective lignin destructor, was purified to a homogeneous state (with an RZ purity index of 1.8) and characterized for the first time. The molecular weight of LiP9 was 43 kDa and its pI was 3.2. The enzyme showed the highest activity at pH 2.5 and 35°C when veratryl alcohol was used as a substrate. The analysis of the substrate specificity showed that LiP9 oxidized phenol derivatives much faster than those of benzoic and cinnamic acids with the same substituents in the benzene ring. The highest specific activity of the enzyme was observed for catechol oxidation. The ability of LiP9 to decolorize recalcitrant dyes (reactive black 5, congo red, remazol brilliant blue R, phenol red, indigo carmine, and bromocresol green) was assessed. The highest decolorization efficiency was shown for indigo carmine (in the presence of veratryl alcohol) and bromocresol green (directly) up to 80 and 60%, respectively, in 1 hour.</p>","PeriodicalId":466,"journal":{"name":"Applied Biochemistry and Microbiology","volume":"60 6","pages":"1209 - 1222"},"PeriodicalIF":1.0000,"publicationDate":"2024-12-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1134/S0003683824605730.pdf","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Applied Biochemistry and Microbiology","FirstCategoryId":"99","ListUrlMain":"https://link.springer.com/article/10.1134/S0003683824605730","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"BIOTECHNOLOGY & APPLIED MICROBIOLOGY","Score":null,"Total":0}
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Abstract
Lignin peroxidase (LiP9) from the basidiomycete Trametes hirsuta LE-BIN 072, an effective lignin destructor, was purified to a homogeneous state (with an RZ purity index of 1.8) and characterized for the first time. The molecular weight of LiP9 was 43 kDa and its pI was 3.2. The enzyme showed the highest activity at pH 2.5 and 35°C when veratryl alcohol was used as a substrate. The analysis of the substrate specificity showed that LiP9 oxidized phenol derivatives much faster than those of benzoic and cinnamic acids with the same substituents in the benzene ring. The highest specific activity of the enzyme was observed for catechol oxidation. The ability of LiP9 to decolorize recalcitrant dyes (reactive black 5, congo red, remazol brilliant blue R, phenol red, indigo carmine, and bromocresol green) was assessed. The highest decolorization efficiency was shown for indigo carmine (in the presence of veratryl alcohol) and bromocresol green (directly) up to 80 and 60%, respectively, in 1 hour.
期刊介绍：
Applied Biochemistry and Microbiology is an international peer reviewed journal that publishes original articles on biochemistry and microbiology that have or may have practical applications. The studies include: enzymes and mechanisms of enzymatic reactions, biosynthesis of low and high molecular physiologically active compounds; the studies of their structure and properties; biogenesis and pathways of their regulation; metabolism of producers of biologically active compounds, biocatalysis in organic synthesis, applied genetics of microorganisms, applied enzymology; protein and metabolic engineering, biochemical bases of phytoimmunity, applied aspects of biochemical and immunochemical analysis; biodegradation of xenobiotics; biosensors; biomedical research (without clinical studies). Along with experimental works, the journal publishes descriptions of novel research techniques and reviews on selected topics.
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