{"title":"黄单胞菌AK几丁质酶ChiA基因的克隆、序列分析及ChiA的一些特性","authors":"Kazuo Sakka , Ryo Kusaka , Akihiro Kawano , Shuichi Karita , Jiraporn Sukhumavasi , Tetsuya Kimura , Kunio Ohmiya","doi":"10.1016/S0922-338X(99)80001-4","DOIUrl":null,"url":null,"abstract":"<div><p>The <em>chiA</em> gene encoding chitinase A was cloned into <em>Escherichia coli</em> from <em>Xanthomonas</em> sp. strain AK and its nucleotide sequence was determined. The structural gene consists of 1788 bp encoding 596 amino acids with a predicted molecular weight of 62,122. The deduced ChiA is a modular enzyme composed of an N-terminal signal peptide and four domains in the following order: a chitin-binding domain, two fibronectin type III domains, and a family 18 catalytic domain. ChiA purified from the recombinant <em>E. coli</em> had temperature and pH optima at 35°C and 4.5, respectively. The <em>K</em><sub>m</sub> and <em>V</em><sub>max</sub> values for colloidal chitin were estimated to be 1.8 mg/ml and 8.7 μmol/min/mg, respectively.</p></div>","PeriodicalId":15696,"journal":{"name":"Journal of Fermentation and Bioengineering","volume":"86 6","pages":"Pages 527-533"},"PeriodicalIF":0.0000,"publicationDate":"1998-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0922-338X(99)80001-4","citationCount":"19","resultStr":"{\"title\":\"Cloning and sequencing of the gene encoding chitinase ChiA from Xanthomonas sp. strain AK and some properties of ChiA\",\"authors\":\"Kazuo Sakka , Ryo Kusaka , Akihiro Kawano , Shuichi Karita , Jiraporn Sukhumavasi , Tetsuya Kimura , Kunio Ohmiya\",\"doi\":\"10.1016/S0922-338X(99)80001-4\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>The <em>chiA</em> gene encoding chitinase A was cloned into <em>Escherichia coli</em> from <em>Xanthomonas</em> sp. strain AK and its nucleotide sequence was determined. The structural gene consists of 1788 bp encoding 596 amino acids with a predicted molecular weight of 62,122. The deduced ChiA is a modular enzyme composed of an N-terminal signal peptide and four domains in the following order: a chitin-binding domain, two fibronectin type III domains, and a family 18 catalytic domain. ChiA purified from the recombinant <em>E. coli</em> had temperature and pH optima at 35°C and 4.5, respectively. The <em>K</em><sub>m</sub> and <em>V</em><sub>max</sub> values for colloidal chitin were estimated to be 1.8 mg/ml and 8.7 μmol/min/mg, respectively.</p></div>\",\"PeriodicalId\":15696,\"journal\":{\"name\":\"Journal of Fermentation and Bioengineering\",\"volume\":\"86 6\",\"pages\":\"Pages 527-533\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1998-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/S0922-338X(99)80001-4\",\"citationCount\":\"19\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of Fermentation and Bioengineering\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S0922338X99800014\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Fermentation and Bioengineering","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0922338X99800014","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Cloning and sequencing of the gene encoding chitinase ChiA from Xanthomonas sp. strain AK and some properties of ChiA
The chiA gene encoding chitinase A was cloned into Escherichia coli from Xanthomonas sp. strain AK and its nucleotide sequence was determined. The structural gene consists of 1788 bp encoding 596 amino acids with a predicted molecular weight of 62,122. The deduced ChiA is a modular enzyme composed of an N-terminal signal peptide and four domains in the following order: a chitin-binding domain, two fibronectin type III domains, and a family 18 catalytic domain. ChiA purified from the recombinant E. coli had temperature and pH optima at 35°C and 4.5, respectively. The Km and Vmax values for colloidal chitin were estimated to be 1.8 mg/ml and 8.7 μmol/min/mg, respectively.
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