| dc.creator | Lin,Ling | |
| dc.creator | Liu,Xiaozhou | |
| dc.creator | Zhou,Yating | |
| dc.creator | Guan,Linyan | |
| dc.creator | Jiajia,He | |
| dc.creator | Huang,Weiqian | |
| dc.date | 2016-11-01 | |
| dc.date.accessioned | 2019-05-03T12:45:27Z | |
| dc.date.available | 2019-05-03T12:45:27Z | |
| dc.identifier | https://scielo.conicyt.cl/scielo.php?script=sci_arttext&pid=S0717-34582016000600009 | |
| dc.identifier.uri | http://revistaschilenas.uchile.cl/handle/2250/85583 | |
| dc.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. | |
| dc.format | text/html | |
| dc.language | en | |
| dc.publisher | Pontificia Universidad Católica de Valparaíso | |
| dc.relation | 10.1016/j.ejbt.2016.09.004 | |
| dc.rights | info:eu-repo/semantics/openAccess | |
| dc.source | Electronic Journal of Biotechnology v.19 n.6 2016 | |
| dc.subject | Protein modeling | |
| dc.subject | Site-directed mutagenesis | |
| dc.subject | Cellulases | |
| dc.subject | Recombinant endoglucanase gene | |
| dc.subject | Catalytic domain ofglycoside hydrolase | |
| dc.subject | Carbohydrate-binding module | |
| dc.subject | High pH stability | |
| dc.subject | Tolerance to deleterious chemicals, Tolerance to heavy metals | |
| dc.subject | Tolerance to detergents | |
| dc.title | A novel pH-stable, endoglucanase (JqCel5A) isolated from a salt-lake microorganism, Jonesia quinghaiensis | |
