A novel, highly efficient β-glucosidase with a cellulose-binding domain: characterization and properties of native and recombinant proteins.

ABSTRACT:

Background

Cellulose, the most abundant biopolymer on earth, is an alternative for fossil fuels as a renewable feedstock for the production of second-generation biofuels and other chemicals. The discovery of novel, highly efficient β-glucosidases remains as one of the major bottlenecks for cellulose degradation. In this context, the ascomycete Talaromyces amestolkiae, isolated from cereal samples, has been studied as a promising source for these enzymes.

Results

BGL-2 is the major β-glucosidase secreted by this fungus in the presence of cellulosic inductors. This enzyme possesses a CBD (Cellulose Binding Domain), an unusual feature among this type of proteins. Besides, when growing on cellulose, the fungus produced two different bgl-2 mRNAs that were clo

SUBMITTER: Mendez-Liter JA 

PROVIDER: S-EPMC5674860 | biostudies-literature | 2017

REPOSITORIES: biostudies-literature