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

作者：Liu, Yun; Dun, Baoqing; Shi, Pengjun; Ma, Rui; Luo, Huiying; Bai, Yingguo; Xie, Xiangming^*; Yao, Bin

来源：PLos One, 2015, 10(9): e0137485.

DOI：10.1371/journal.pone.0137485

• CLONING
• ENDOGLUCANASES
• PURIFICATION
• DEGRADATION
• CELLULOSE

An endo-beta-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 fulllength 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 degrees C, respectively, and showed broad pH adaptability (pH 3.0-6.0) and excellent stability at pH3.0-8.0 and 60 degrees C. Belonging to the group of nonspecific endoglucanases, Cel7A exhibited the highest activity on barley beta-glucan (2020 +/- 9 Umg(-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 mu 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.

• 出版日期2015-9-11
• 单位中国农业科学院; 北京林业大学