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


Autoři: Yuan Gu aff001;  Fei Zheng aff001;  Yuan Wang aff001;  Xiaoyun Su aff001;  Yingguo Bai aff001;  Bin Yao aff001;  Huoqing Huang aff001;  Huiying Luo aff001
Působiště autorů: Key Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing, People’s Republic of China aff001;  College of Biological Sciences and Biotechnology, Beijing Forestry University, Beijing, People’s Republic of China aff002
Vyšlo v časopise: PLoS ONE 14(11)
Kategorie: Research Article
doi: 10.1371/journal.pone.0224803

Souhrn

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.

Klíčová slova:

Barley – Cellulases – Cellulose – Glucose – Hydrolysis – Multiple alignment calculation – Sequence alignment – Lichenology


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