A thermophilic endo-1,4-beta-glucanase from Talaromyces emersonii CBS394.64 with broad substrate specificity and great application potentials

作者：Wang, Kun; Luo, Huiying^*; Bai, Yingguo; Shi, Pengjun; Huang, Huoqing; Xue, Xianli; Yao, Bin

来源：Applied Microbiology and Biotechnology, 2014, 98(16): 7051-7060.

DOI：10.1007/s00253-014-5680-0

• Talaromyces emersonii
• Endo-1,4-beta-glucanase
• Thermophilic
• Broad substrate specificity

Thermophilic cellulases are of significant interest to the efficient conversion of plant cell wall polysaccharides into simple sugars. In this study, a thermophilic and thermostable endo-1,4-beta-glucanase, TeEgl5A, was identified in the thermophilic fungus Talaromyces emersonii CBS394.64 and functionally expressed in Pichia pastoris. Purified recombinant TeEgl5A exhibits optimal activity at pH 4.5 and 90 A degrees C. It is highly stable at 70 A degrees C and over a broad pH range of 1.0-10.0, and shows strong resistance to most metal ions, sodium dodecyl sulfate (SDS), and proteases. TeEgl5A has broad substrate specificity and exhibits high activity on substrates containing beta-1,4-glycosidic bonds and beta-1,3-glycosidic bonds (barley beta-glucan, laminarin, lichenan, CMC-Na, carob bean gum, and birchwood xylan). Under simulated mashing conditions, addition of 60 U TeEgl5A reduced more viscosity (10.0 vs.7.6 %) than 80 U of Ultraflo XL from Novozymes. These properties make TeEgl5A a good candidate for extensive application in the detergent, textile, feed, and food industries.

• 出版日期2014-8
• 单位中国农业科学院