The enzymatic characters of heterologous expressed novel β-1, 4-glucosidase originated from Aspergillus fresenii

β-1, 4-glucosidases generate glucose from cellobiose and oligosaccharides, enhancing the productivity in biorefinery and the bioconversion process as well as the nutritional value in food and feed. With the high-throughput sequencing technique, a novel β-1, 4-glucosidase, named bglT2, containing 861 amino acid residues, was found from Aspergillus fresenii. bglT2 belongs to the glycosyl hydrolase (GH) family 3. The bglT2 that expressed by Komagataella phaffiiX33 presented the highest activity at 55 °C and pH 5.5. The half-lives of bglT2 under 50 °C, 55 °C, 60 °C, and 65 °C were 9 min 36 s, 4 min 22 s, 117 s, and 68 s, respectively. The bglT2 was stable between pH 3.0 to pH 8.0. The Michaelis constant (Km) and the theoretical maximum rate (Vmax) of bglT2 were 0.0007 mol/L and 9 × 10−8mol/L/s, respectively. In a 5 L fermentation vessel, the recombinant K.phaffiiX33 could yield a β-1, 4-glucosidase activity of 4.45 U/mL after 96 h methanol inducement. As an important member of cellulases, the novel bglT2 might contribute to bioenergy, food processing, feed enrichment, and nutritional study, etc. This study also developed a path to obtain new enzymes depending on high-throughput sequencing technique.