[Credit:Biotechnology for Biofuels]
Molecular surface model of BGL-2 from T. amestolkiae. The catalytic domain (grey), the connector (blue, red and white) and the CBD (blue) are depicted. [Credit:Biotechnology for Biofuels]
05 Dec 2017
A novel and highly efficient fungal β-glucosidase characterized

The current need of finding sustainable and renewable energy sources is making the enzymatic degradation of plant biomass to produce second-generation biofuels a blooming subject, since they may represent a green-viable alternative to fossil fuels.

β-glucosidases are considered as the key enzymes for this process because they are indispensible for releasing free glucose from cellulose, the major plant cell polysaccharide and the most abundant organic compound on earth.

In a new study published in the journal Biotechnology for Biofuels and carried out by the group of Biotechnology for Lignocellulosic Biomass lead by Dr. María Jesús Martínez, the characterization and properties of a β-glucosidase form the ascomycete Talaromyces amestolkiae have been presented.

This enzyme (BGL-2) stands out for being the first 1,4-β-glucosidase with a functional cellulose binding domain (CBD), an unusual feature among this type of proteins although it has been reported  in other cellulolytic enzymes, such as cellobiohydrolases and 1,4-β-endoglucanases. The work has revealed the high potential of the native BGL-2 and its recombinant forms, with and without CBD, to be applied for the saccharification of plant biomass being very efficient using cellobiose and other short oligosaccharides as substrate, with similar efficiency to other β-glucosidases present in commercial cocktails.

The complete characterization of the cellulolytic system of T. amestolkiae is currently being carried out, with special interest in the characterization of other β-glucosidases produced by this strain, to evaluate their properties and features to be used in different biotechnological applications.

Reference: A novel, highly efficient β-glucosidase with a cellulose-binding domain: characterization and properties of native and recombinant proteins. Méndez-Líter JA, Gil-Muñoz J, Nieto-Domínguez M, Barriuso J, de Eugenio LI, Martínez MJ. Biotechnology for Biofuels. 2017;10:256. doi:10.1186/s13068-017-0946-2.