IQUIBICEN   23947
INSTITUTO DE QUIMICA BIOLOGICA DE LA FACULTAD DE CIENCIAS EXACTAS Y NATURALES
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
Building the molecular blocks of multi-enzymatic complexes for the improvement of biofuel production
Autor/es:
IGLESIAS RANDO MR; ZYLBERMAN V; GOROJOVSKY N; DODES M; CRAIG PO; SANTOS J; GOLDBAUM FA
Lugar:
Buenos Aires
Reunión:
Congreso; Reunión Conjunta de Sociedades de Biociencias y XLVI Reunión Anual de la Sociedad Argentina de Biofísica (SAB); 2017
Institución organizadora:
Sociedad Argentina de Biofisica y otras sociedades cientificas SAIB, SAIC, etc
Resumen:
The enzymatic degradation of lignocellulose generates sugars that upon fermentation produce bioethanol. The enzymes currently used in this process are expensive and have low efficiency. It is important to develop new methods to increase the activity and stability of these enzymes for an economically viable production bioethanol. 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 use the structure of an oligomeric protein that is highly stable and highly expressed in bacteria, as a scaffold for the colocalization of a consortium of cellulolytic enzymes and the development of artificial cellulosomes. For the assembly of these multienzymatic particles we use a non-covalent coupling strategy trough high affinity heterodimeric peptides complementary fused to the oligomeric scaffold and the target enzymes. For this purpose we cloned and expressed in E.Coli the catalytic domain of a variety of enzymes, including endocglucanases, exoglucanases, xylanases, beta glucosidases and cellulose binding domains from different organisms, fused to the coupling peptide. The amount and solubility of these multienzyme building blocks were compared to the original isolated domains. The coupling peptide doesn?t perturb the solubility of the target proteins. At least one member of each functional category is solubly expressed in significant amounts, encouraging further development of the artificial cellulosomes. 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.