RRC ID 60634
Author Gu Y, Zheng F, Wang Y, Su X, Bai Y, Yao B, Huang H, Luo H.
Title Characterization of two thermophilic cellulases from Talaromyces leycettanus JCM12802 and their synergistic action on cellulose hydrolysis.
Journal PLoS ONE
Abstract 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.
Volume 14(11)
Pages e0224803
Published 2019
DOI 10.1371/journal.pone.0224803
PII PONE-D-19-21437
PMID 31730665
PMC PMC6857856
MeSH Amino Acid Sequence Cellulases / chemistry Cellulases / metabolism* Cellulose / metabolism* Enzyme Stability Hydrogen-Ion Concentration Hydrolysis Kinetics Recombinant Proteins / isolation & purification Recombinant Proteins / metabolism Substrate Specificity Talaromyces / enzymology* Temperature*
IF 2.776
Times Cited 1
Resource
General Microbes JCM12802