{"title":"嗜碱芽孢杆菌菌株41M-1木聚糖酶J的定向进化:最适酸性条件下突变体嗜碱性的恢复","authors":"Mayuko Inami, Chihiro Morokuma, Akiko Sugio, Hidenori Tamanoi, Rie Yatsunami, Satoshi Nakamura","doi":"10.1093/nass/3.1.315","DOIUrl":null,"url":null,"abstract":"<p><p>Alkaliphilic Bacillus sp. strain 41M-1 produces an alkaliphilic xylanase (xylanase J). The newly constructed mutant E177Q deltaJC had an acidic pH optimum and showed almost no activity at pH 8.0. The alkaliphily of the enzyme was restored by directed evolution. The evolved mutants, Y176S/E177Q deltaJC and G32V/Y176D/E177Q deltaJC, retained about 30% and 43% activity of their maximal activities at pH 6.0, respectively.</p>","PeriodicalId":86149,"journal":{"name":"Nucleic acids research. Supplement (2001)","volume":" 3","pages":"315-6"},"PeriodicalIF":0.0000,"publicationDate":"2003-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1093/nass/3.1.315","citationCount":"14","resultStr":"{\"title\":\"Directed evolution of xylanase J from alkaliphilic Bacillus sp. strain 41M-1: restore of alkaliphily of a mutant with an acidic pH optimum.\",\"authors\":\"Mayuko Inami, Chihiro Morokuma, Akiko Sugio, Hidenori Tamanoi, Rie Yatsunami, Satoshi Nakamura\",\"doi\":\"10.1093/nass/3.1.315\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Alkaliphilic Bacillus sp. strain 41M-1 produces an alkaliphilic xylanase (xylanase J). The newly constructed mutant E177Q deltaJC had an acidic pH optimum and showed almost no activity at pH 8.0. The alkaliphily of the enzyme was restored by directed evolution. The evolved mutants, Y176S/E177Q deltaJC and G32V/Y176D/E177Q deltaJC, retained about 30% and 43% activity of their maximal activities at pH 6.0, respectively.</p>\",\"PeriodicalId\":86149,\"journal\":{\"name\":\"Nucleic acids research. Supplement (2001)\",\"volume\":\" 3\",\"pages\":\"315-6\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2003-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1093/nass/3.1.315\",\"citationCount\":\"14\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Nucleic acids research. Supplement (2001)\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1093/nass/3.1.315\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Nucleic acids research. Supplement (2001)","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1093/nass/3.1.315","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Directed evolution of xylanase J from alkaliphilic Bacillus sp. strain 41M-1: restore of alkaliphily of a mutant with an acidic pH optimum.
Alkaliphilic Bacillus sp. strain 41M-1 produces an alkaliphilic xylanase (xylanase J). The newly constructed mutant E177Q deltaJC had an acidic pH optimum and showed almost no activity at pH 8.0. The alkaliphily of the enzyme was restored by directed evolution. The evolved mutants, Y176S/E177Q deltaJC and G32V/Y176D/E177Q deltaJC, retained about 30% and 43% activity of their maximal activities at pH 6.0, respectively.
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