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A novel pH-stable, endoglucanase (JqCel5A) isolated from a salt-lake microorganism, Jonesia quinghaiensis Electron. J. Biotechnol.
Lin,Ling; Liu,Xiaozhou; Zhou,Yating; Guan,Linyan; Jiajia,He; Huang,Weiqian.
Background: Endoglucanase, one of three type cellulases, can randomly cleave internal p-1,4-linkages in cellulose polymers. Thus, it could be applied in agricultural and industrial processes. Results: A novel endoglucanase gene (JqCel5A) was cloned from Jonesia quinghaiensis and functionally expressed in Escherichia coli Rosetta (DE3). It contained 1722 bp and encoded a 573-residue polypeptide consisting of a catalytic domain of glycoside hydrolase family 5 (GH5) and a type 2 carbohydrate-binding module (CBM2), together with a predicted molecular mass of 61.79 kD. The purified JqCel5A displayed maximum activity at 55°C and pH 7.0, with 21.7 U/mg, 26.19 U/mg and 4.81 U/mg towards the substrate carboxymethyl cellulose, barley glucan and filter paper,...
Tipo: Journal article Palavras-chave: Protein modeling Site-directed mutagenesis Cellulases Recombinant endoglucanase gene Catalytic domain ofglycoside hydrolase Carbohydrate-binding module High pH stability Tolerance to deleterious chemicals; Tolerance to heavy metals Tolerance to detergents.
Ano: 2016 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582016000600009
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