{"title":"探索、克隆和鉴定用于生产β-苯乙醇的芳基乙醇脱氢酶","authors":"Z. Zhou, Y. Zhao, D. Peng, Z. Wu, W. Zhang","doi":"10.1134/S0003683823602329","DOIUrl":null,"url":null,"abstract":"<p>β-Phenylethanol is the primary flavor compound in Sichuan industrial paocai. Metatranscriptomics analysis revealed that the gene encoding aryl-alcohol dehydrogenase (<i>AADh1</i>), which is responsible for β-phenylethanol synthesis, had the highest expression level during the late stage of fermentation (180 days). In the present study, we explored the potential <i>AADh1</i> in Sichuan industrial qingcai paocai by combining metatranscriptomics results and <i>AADh1</i> analysis in NCBI. <i>AADh1</i> was successfully cloned and expressed in <i>Escherichia coli</i> BL21, and the enzymatic properties of AADh1 were characterized. AADh1 exhibited the highest activity at pH 7.0 and 50°C, with the highest stability at pH 8.0 and 25°C. Furthermore, the enzyme exhibited low tolerance to metal ions, and only 1 mM Mn<sup>2+</sup> could slightly activate the enzyme. Moreover, AADh1 was successfully used to preliminarily enhance the β-phenylethanol of industrial paocai, which could improve the flavor of paocai to a certain extent in practical production.</p>","PeriodicalId":466,"journal":{"name":"Applied Biochemistry and Microbiology","volume":null,"pages":null},"PeriodicalIF":1.0000,"publicationDate":"2024-03-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Exploring, Cloning, and Characterization of Aryl-alcohol Dehydrogenase for β-Phenylethanol Production in Paocai\",\"authors\":\"Z. Zhou, Y. Zhao, D. Peng, Z. Wu, W. Zhang\",\"doi\":\"10.1134/S0003683823602329\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p>β-Phenylethanol is the primary flavor compound in Sichuan industrial paocai. Metatranscriptomics analysis revealed that the gene encoding aryl-alcohol dehydrogenase (<i>AADh1</i>), which is responsible for β-phenylethanol synthesis, had the highest expression level during the late stage of fermentation (180 days). In the present study, we explored the potential <i>AADh1</i> in Sichuan industrial qingcai paocai by combining metatranscriptomics results and <i>AADh1</i> analysis in NCBI. <i>AADh1</i> was successfully cloned and expressed in <i>Escherichia coli</i> BL21, and the enzymatic properties of AADh1 were characterized. AADh1 exhibited the highest activity at pH 7.0 and 50°C, with the highest stability at pH 8.0 and 25°C. Furthermore, the enzyme exhibited low tolerance to metal ions, and only 1 mM Mn<sup>2+</sup> could slightly activate the enzyme. Moreover, AADh1 was successfully used to preliminarily enhance the β-phenylethanol of industrial paocai, which could improve the flavor of paocai to a certain extent in practical production.</p>\",\"PeriodicalId\":466,\"journal\":{\"name\":\"Applied Biochemistry and Microbiology\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":1.0000,\"publicationDate\":\"2024-03-27\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Applied Biochemistry and Microbiology\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://link.springer.com/article/10.1134/S0003683823602329\",\"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}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Applied Biochemistry and Microbiology","FirstCategoryId":"99","ListUrlMain":"https://link.springer.com/article/10.1134/S0003683823602329","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}
Exploring, Cloning, and Characterization of Aryl-alcohol Dehydrogenase for β-Phenylethanol Production in Paocai
β-Phenylethanol is the primary flavor compound in Sichuan industrial paocai. Metatranscriptomics analysis revealed that the gene encoding aryl-alcohol dehydrogenase (AADh1), which is responsible for β-phenylethanol synthesis, had the highest expression level during the late stage of fermentation (180 days). In the present study, we explored the potential AADh1 in Sichuan industrial qingcai paocai by combining metatranscriptomics results and AADh1 analysis in NCBI. AADh1 was successfully cloned and expressed in Escherichia coli BL21, and the enzymatic properties of AADh1 were characterized. AADh1 exhibited the highest activity at pH 7.0 and 50°C, with the highest stability at pH 8.0 and 25°C. Furthermore, the enzyme exhibited low tolerance to metal ions, and only 1 mM Mn2+ could slightly activate the enzyme. Moreover, AADh1 was successfully used to preliminarily enhance the β-phenylethanol of industrial paocai, which could improve the flavor of paocai to a certain extent in practical production.
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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