A novel pH-stable, endoglucanase (JqCel5A) isolated from a salt-lake microorganism, Jonesia quinghaiensis
Electron. j. biotechnol
; Electron. j. biotechnol;19(6): 56-62, Nov. 2016. ilus
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| ID: biblio-840314
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ABSTRACT
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.Palavras-chave
Texto completo:
1
Índice:
LILACS
Assunto principal:
Actinomycetales
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Celulases
Tipo de estudo:
Prognostic_studies
Idioma:
En
Revista:
Electron. j. biotechnol
Assunto da revista:
BIOTECNOLOGIA
Ano de publicação:
2016
Tipo de documento:
Article
/
Project document