Development of multi-enzymatic complexes for the improvement of biofuel production

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

Tucuman

Congreso; III Latin American Federation of Biophysical Societies (LAFeBS), IX Ibero American Congress of Biophysics, XLV Reunion Annual SAB 2016; 2016

Sociedad Argentina de Biofisica (SAB)

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/dockerina 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.