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| 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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| Lin,Ling; Kan,Xianzhao; Yan,Hao; Wang,Danni. |
| The gram-positive spore-forming bacteria, Bacillus thuringiensis (Bt) strains produced novel cellulases which could liberate glucose from soluble cellulose, carboxymethyl cellulose (CMC), and insoluble crystalline cellulose. The maximal cellulase activities were obtained after 60 hrs incubation at 28ºC in a LB broth medium with 1% CMC. Maximum CMCase activities were got at 40ºC and pH 4.0, respectively, and more than 50% of its maximal activity was retained at 40-60ºC for 1 hr, while approximately 40% of its maximal activity was also retained after incubating at 70ºC for 1 hr. Most metal ions and reagents such as Ca2+, Mg2+, Cd2+, Pb2+, Zn2+, Cu2+, EDTA, and SDS inhibited the enzyme activities, but K+ and Mn2+ activated the activities. The enzymes from... |
| Tipo: Journal article |
Palavras-chave: Bacillus thuringiensis; Cellulase; Cellulose-degrading; Characterization. |
| Ano: 2012 |
URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582012000300002 |
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