A novel pH-stable, endoglucanase (JqCel5A) isolated from a salt-lake microorganism, Jonesia quinghaiensis

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 express...

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Autores principales:	Lin,Ling, Liu,Xiaozhou, Zhou,Yating, Guan,Linyan, Jiajia,He, Huang,Weiqian
Lenguaje:	English
Publicado:	Pontificia Universidad Católica de Valparaíso 2016
Materias:	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
Acceso en línea:	http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582016000600009
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spelling	oai:scielo:S0717-345820160006000092017-01-25A novel pH-stable, endoglucanase (JqCel5A) isolated from a salt-lake microorganism, Jonesia quinghaiensisLin,LingLiu,XiaozhouZhou,YatingGuan,LinyanJiajia,HeHuang,Weiqian 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 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, respectively. Interestingly, JqCel5A exhibited high pH stability over a broad pH range of pH (3-11), and had good tolerance to a wide variety of deleterious chemicals including heavy metals and detergent. The catalytic mechanism of JqCel5A was also investigated by site mutagenesis and homology-modeling in this study. Conclusions: It was believed that these properties might make JqCel5A to be potentially used in the suitable industrial catalytic condition, which has a broad pH fluctuation and/or chemical disturbance.info:eu-repo/semantics/openAccessPontificia Universidad Católica de ValparaísoElectronic Journal of Biotechnology v.19 n.6 20162016-11-01text/htmlhttp://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582016000600009en10.1016/j.ejbt.2016.09.004
institution	Scielo Chile
collection	Scielo Chile
language	English
topic	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
spellingShingle	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 Lin,Ling Liu,Xiaozhou Zhou,Yating Guan,Linyan Jiajia,He Huang,Weiqian A novel pH-stable, endoglucanase (JqCel5A) isolated from a salt-lake microorganism, Jonesia quinghaiensis
description	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, respectively. Interestingly, JqCel5A exhibited high pH stability over a broad pH range of pH (3-11), and had good tolerance to a wide variety of deleterious chemicals including heavy metals and detergent. The catalytic mechanism of JqCel5A was also investigated by site mutagenesis and homology-modeling in this study. Conclusions: It was believed that these properties might make JqCel5A to be potentially used in the suitable industrial catalytic condition, which has a broad pH fluctuation and/or chemical disturbance.
author	Lin,Ling Liu,Xiaozhou Zhou,Yating Guan,Linyan Jiajia,He Huang,Weiqian
author_facet	Lin,Ling Liu,Xiaozhou Zhou,Yating Guan,Linyan Jiajia,He Huang,Weiqian
author_sort	Lin,Ling
title	A novel pH-stable, endoglucanase (JqCel5A) isolated from a salt-lake microorganism, Jonesia quinghaiensis
title_short	A novel pH-stable, endoglucanase (JqCel5A) isolated from a salt-lake microorganism, Jonesia quinghaiensis
title_full	A novel pH-stable, endoglucanase (JqCel5A) isolated from a salt-lake microorganism, Jonesia quinghaiensis
title_fullStr	A novel pH-stable, endoglucanase (JqCel5A) isolated from a salt-lake microorganism, Jonesia quinghaiensis
title_full_unstemmed	A novel pH-stable, endoglucanase (JqCel5A) isolated from a salt-lake microorganism, Jonesia quinghaiensis
title_sort	novel ph-stable, endoglucanase (jqcel5a) isolated from a salt-lake microorganism, jonesia quinghaiensis
publisher	Pontificia Universidad Católica de Valparaíso
publishDate	2016
url	http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582016000600009
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A novel pH-stable, endoglucanase (JqCel5A) isolated from a salt-lake microorganism, Jonesia quinghaiensis

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