{"title":"二苯并噻吩脱硫酶的纯化、表征及结晶。","authors":"T Ohshiro, Y Izumi","doi":"10.1023/a:1008181730720","DOIUrl":null,"url":null,"abstract":"<p><p>DszC and DszA, DBT monooxygenase and DBT sulfone monooxygenase, respectively, involved in dibenzothiophene (DBT) desulfurization, were purified to homogeneity from Rhodococcus erythropolis D-1. The two enzymes were crystallized and enzymologically characterized. We found a high activity of flavin reductase in the non-DBT-desulfurizing bacterium, Paenibacillus polymyxa A-1, which is essential for DszC and A activities, and purified to homogeneity and characterized the enzyme.</p>","PeriodicalId":9179,"journal":{"name":"Bioseparation","volume":"9 3","pages":"185-8"},"PeriodicalIF":0.0000,"publicationDate":"2000-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1023/a:1008181730720","citationCount":"15","resultStr":"{\"title\":\"Purification, characterization and crystallization of enzymes for dibenzothiophene desulfurization.\",\"authors\":\"T Ohshiro, Y Izumi\",\"doi\":\"10.1023/a:1008181730720\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>DszC and DszA, DBT monooxygenase and DBT sulfone monooxygenase, respectively, involved in dibenzothiophene (DBT) desulfurization, were purified to homogeneity from Rhodococcus erythropolis D-1. The two enzymes were crystallized and enzymologically characterized. We found a high activity of flavin reductase in the non-DBT-desulfurizing bacterium, Paenibacillus polymyxa A-1, which is essential for DszC and A activities, and purified to homogeneity and characterized the enzyme.</p>\",\"PeriodicalId\":9179,\"journal\":{\"name\":\"Bioseparation\",\"volume\":\"9 3\",\"pages\":\"185-8\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2000-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1023/a:1008181730720\",\"citationCount\":\"15\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Bioseparation\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1023/a:1008181730720\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Bioseparation","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1023/a:1008181730720","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 15
摘要
从红红红球菌D-1中纯化出参与二苯并噻吩(DBT)脱硫的DszC和DszA，分别为DBT单加氧酶和DBT砜单加氧酶。对这两种酶进行了结晶和酶学表征。我们在非dbt脱硫菌Paenibacillus polymyxa a -1中发现了高活性的黄素还原酶，该酶对DszC和a的活性至关重要，并对其进行了纯化和表征。
Purification, characterization and crystallization of enzymes for dibenzothiophene desulfurization.
DszC and DszA, DBT monooxygenase and DBT sulfone monooxygenase, respectively, involved in dibenzothiophene (DBT) desulfurization, were purified to homogeneity from Rhodococcus erythropolis D-1. The two enzymes were crystallized and enzymologically characterized. We found a high activity of flavin reductase in the non-DBT-desulfurizing bacterium, Paenibacillus polymyxa A-1, which is essential for DszC and A activities, and purified to homogeneity and characterized the enzyme.
京公网安备 11010802042870号
京ICP备2023020795号-1
分享
求助内容：
应助结果提醒方式：
扫码关注我们
