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In this study, we isolated and identified a thermophilic strain of Aspergillus fumigatus from the “Daqu” samples. Transcriptomic analysis of A. fumigatus identified 239 carbohydrate-active enzymes (CAZy)-encoding genes, including 167 glycoside hydrolase (GH)-encoding genes, 58 glycosyltransferase (GT)-encoding genes, 2 polysaccharide lyase (PLs)-encoding genes and 12 carbohydrate esterase (CEs)-encoding genes, which indicates that the strain has a strong potential for application for enzyme production. Furthermore, we also identified a novel endoglucanase gene (AfCel5A), which was expressed in Pichia pastoris and characterized. The novel endoglucanase AfCel5A exhibited the highest hydrolytic activity against CMC-Na and the optimal activity at 80 °C and pH 4.0 and also showed good stability at pH 3.0–11.0 and below 70 °C. The Km and Vmax values of AfCel5 were 0.16 ± 0.05 mg·mL−1 and 7.23 ± 0.33 mol mg−1·min−1, respectively, using CMC-Na as a substrate. Further, the endoglucanase exhibited a high tolerance toward NaCl as well as glucose. In addition, the finding that the endoglucanase AfCel5A in combination with β-mannanse (ManBK) clearly increased the release of total reducing sugars of glucomannan by up to 74% is significant.

A Thermophilic GH5 Endoglucanase from Aspergillus fumigatus and Its Synergistic Hydrolysis of Mannan-Containing Polysaccharides