IQUIBICEN   23947
INSTITUTO DE QUIMICA BIOLOGICA DE LA FACULTAD DE CIENCIAS EXACTAS Y NATURALES
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
Production of artificial cellulosomes to improve lignocellulose degradation: a step towards clean energy
Autor/es:
GOROJOVSKY, N; IGLESIAS RANDO, MR; CRAIG, PO; GOLDBAUM FA
Lugar:
Virtual
Reunión:
Simposio; Biocatalysis Open day; 2020
Institución organizadora:
Organizado por European Federation of Biotechnology (EFB)
Resumen:
Lignocellulose enzymatic degradation generates sugars that upon fermentation produce bioethanol. For an economically viable production of bioethanol it is essential to develop new methods to increase the activity and stability of the enzymes involved. The cellulosomes of some anaerobic organisms represent the most efficient machinery for lignocellulose degradation. These multienzymatic complexes co-localize different cellulolytic enzymes and cellulose binding domains, increasing their degradation activity through enzymatic proximity and substrate targeting effects. However, the biological production of natural cellulosomes on an industrial scale has serious limitations. Our goal is to develop artificial cellulosomes using an oligomeric protein scaffold that is highly stable and highly expressed in bacteria for the co-localization of various enzymes. For the assembly of these multienzymatic particles we use a non-covalent coupling strategy through high affinity heterodimeric cohesin and dockerin modules, complementary fused to the scaffold subunits and the target proteins, respectively. In this work, we focus on the structural and functional characterization of a monospecific cellulosome composed of an endoglucanase. The polymeric display of the endoglucanase on the structural scaffold produces an increment in the degradation rate of cellulose compared to the free enzyme. This phenomenon seems to be related to an increase in the binding strength of the multienzymatic complex to the substrate due to an avidity effect. In addition, an increment in the thermal stability of the enzyme coupled to the scaffold compared to the free enzyme was observed. We are making progress in the simultaneous coupling of a variety of enzymes to the scaffold. It is expected that this technology would be valuable to improve lignocellulose degradation.