Improving lignocellulose degradation through multienzimatic complexes

GOROJOVSKY, N; IGLESIAS RANDO, MR; GARRONE NA.; SANTOS, J; DODES, M; ZYLBERMAN, V; GOLDBAUM FA.; CRAIG PO.

CABA

Congreso; 2nd Protein Biophysics at the end of the world; 2017

Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, ANPCyT, PABMB, Biophysical Society

Lignocellulose is the most abundant renewable resource on the planet and is an excellent substrate for the production of biofuels. Its enzymatic degradation generates sugars that upon fermentation produce bioethanol. The ligno-cellulolytic enzymes currently used in this process are expensive and have low efficiency. For an economically viable production of biofuels it is essential to develop new methods to increase the activity and stability of these enzymes.Cellulosomes are multienzymatic complexes that colocalize different cellulolytic enzymes and cellulose binding domains, increasing their degradation activity through enzymatic proximity and substrate targeting effects. However, the industrial production of natural cellulosomes has serious limitations because of the properties of their scaffolding protein. Our goal is to develop artificial cellulosomes using the structure of an oligomeric protein that is highly stable and highly expressed in bacteria, as a scaffold for the colocalization of cellulases, hemicellulases, beta-glucosidases and cellulose binding domains. For the assembly of these multienzymatic particles we use a non-covalent coupling strategy trough high affinity heterodimeric modules (coiled peptides or cohesin/dockerin modules) complementary fused to the structure of the protein targets and the oligomeric scaffold. It is expected that these complexes will help to increase the enzymatic lignocellulose degradation, reducing the cost of bioethanol production and favoring fossil fuels substitution.