Characterization of two thermophilic cellulases from Talaromyces leycettanus JCM12802 and their synergistic action on cellulose hydrolysis

Y Gu, F Zheng, Y Wang, X Su, Y Bai, B Yao, H Huang… - Plos one, 2019 - journals.plos.org
Y Gu, F Zheng, Y Wang, X Su, Y Bai, B Yao, H Huang, H Luo
Plos one, 2019journals.plos.org
Talaromyces leycettanus JCM12802 is a great producer of thermophilic glycoside
hydrolases (GHs). In this study, two cellulases (Tl Cel5A and Tl Cel6A) belonging to GH5
and GH6 respectively were expressed in Pichia pastoris and functionally characterized. The
enzymes had acidic and thermophilic properties, showing optimal activities at pH 3.5–4.5
and 75–80° C, and retained stable at temperatures up to 60° C and over a broad pH range
of 2.0− 8.0. Tl Cel5A and Tl Cel6A acted against several cellulose substrates with varied …
Talaromyces leycettanus JCM12802 is a great producer of thermophilic glycoside hydrolases (GHs). In this study, two cellulases (TlCel5A and TlCel6A) belonging to GH5 and GH6 respectively were expressed in Pichia pastoris and functionally characterized. The enzymes had acidic and thermophilic properties, showing optimal activities at pH 3.5–4.5 and 75–80°C, and retained stable at temperatures up to 60°C and over a broad pH range of 2.0−8.0. TlCel5A and TlCel6A acted against several cellulose substrates with varied activities (3,101.1 vs. 92.9 U/mg to barley β-glucan, 3,905.6 U/mg vs. 109.0 U/mg to lichenan, and 840.3 and 0.09 U/mg to CMC-Na). When using Avicel, phosphoric acid swollen cellulose (PASC) or steam-exploded corn straw (SECS) as the substrate, combination of TlCel5A and TlCel6A showed significant synergistic action, releasing more reduced sugars (1.08–2.87 mM) than the individual enzymes. These two cellulases may represent potential enzyme additives for the efficient biomass conversion and bioethanol production.
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