Unknown

Dataset Information

0

A Novel GH7 Endo-?-1,4-Glucanase from Neosartorya fischeri P1 with Good Thermostability, Broad Substrate Specificity and Potential Application in the Brewing Industry.


ABSTRACT: An endo-?-1,4-glucanase gene, cel7A, was cloned from the thermophilic cellulase-producing fungus Neosartorya fischeri P1 and expressed in Pichia pastoris. The 1,410-bp full-length gene encodes a polypeptide of 469 amino acids consisting of a putative signal peptide at residues 1-20, a catalytic domain of glycoside hydrolase family 7 (GH7), a short Thr/Ser-rich linker and a family 1 carbohydrate-binding module (CBM 1). The purified recombinant Cel7A had pH and temperature optima of pH 5.0 and 60°C, respectively, and showed broad pH adaptability (pH 3.0-6.0) and excellent stability at pH3.0-8.0 and 60°C. Belonging to the group of nonspecific endoglucanases, Cel7A exhibited the highest activity on barley ?-glucan (2020 ± 9 U mg-1), moderate on lichenan and CMC-Na, and weak on laminarin, locust bean galactomannan, Avicel, and filter paper. Under simulated mashing conditions, addition of Cel7A (99 ?g) reduced the mash viscosity by 9.1% and filtration time by 24.6%. These favorable enzymatic properties make Cel7A as a good candidate for applications in the brewing industry.

SUBMITTER: Liu Y 

PROVIDER: S-EPMC4567307 | biostudies-literature | 2015

REPOSITORIES: biostudies-literature

altmetric image

Publications

A Novel GH7 Endo-β-1,4-Glucanase from Neosartorya fischeri P1 with Good Thermostability, Broad Substrate Specificity and Potential Application in the Brewing Industry.

Liu Yun Y   Dun Baoqing B   Shi Pengjun P   Ma Rui R   Luo Huiying H   Bai Yingguo Y   Xie Xiangming X   Yao Bin B  

PloS one 20150911 9


An endo-β-1,4-glucanase gene, cel7A, was cloned from the thermophilic cellulase-producing fungus Neosartorya fischeri P1 and expressed in Pichia pastoris. The 1,410-bp full-length gene encodes a polypeptide of 469 amino acids consisting of a putative signal peptide at residues 1-20, a catalytic domain of glycoside hydrolase family 7 (GH7), a short Thr/Ser-rich linker and a family 1 carbohydrate-binding module (CBM 1). The purified recombinant Cel7A had pH and temperature optima of pH 5.0 and 60°  ...[more]

Similar Datasets

| S-EPMC3318711 | biostudies-literature
| S-EPMC4154733 | biostudies-literature
| S-EPMC4491047 | biostudies-literature
| S-EPMC7822948 | biostudies-literature
| S-EPMC3819015 | biostudies-literature
| S-EPMC3795549 | biostudies-literature
| S-EPMC4371660 | biostudies-literature
| S-EPMC7237641 | biostudies-literature
| S-EPMC4583671 | biostudies-literature
| S-EPMC5434006 | biostudies-literature