Carbohydrate binding modules enhance cellulose enzymatic hydrolysis by increasing access of cellulases to the substrate

Autor(es)

Bernardes, A. ^[1] ; Pellegrini, V. O. A. ^[1] ; Curtolo, F. ^[1] ; Camilo, C. M. ^[1] ; Mello, B. L. ^[1] ; Johns, M. A. ^{[2, 3, 4]} ; Scott, J. L. ^{[5, 6]} ; Guimaraes, F. E. C. ^[1] ; Polikarpov, I. ^[1]

Afiliação do(s) autor(es)

^[1] Univ Sao Paulo, Sao Carlos Inst Phys, Ave Trabalhador Sao Carlense 400, BR-13566590 Sao Carlos, SP - Brazil

^[2] Univ Bath, Dept Chem Engn, Bath BA2 7AY, Avon - England

^[3] Univ Bath, EPSRC Ctr Doctoral Training Sustainable Chem Tech, Bath BA2 7AY, Avon - England

^[4] Univ Bristol, Dept Aerosp Engn, Queens Bldg, Bristol BS8 1TR, Avon - England

^[5] Univ Bath, Dept Chem, Bath BA2 7AY, Avon - England

^[6] Univ Bath, Ctr Sustainable Chem Technol, Bath BA2 7AY, Avon - England

• Tipo de documento: Artigo Científico
• Fonte: Carbohydrate Polymers; v. 211, p. 57-68, MAY 1 2019.
• Citações Web of Science: 4

Resumo

Plant biomass is a low-cost and abundant source of carbohydrates for production of fuels, ``green{''} chemicals and materials. Currently, biochemical conversion of the biomass into sugars via enzymatic hydrolysis is the most viable technology. Here, the role of carbohydrate binding modules (CBMs) in the disruption of insoluble polysaccharide structures and their capacity to enhance cellulase-promoted lignocellulosic biomass hydrolysis was investigated. We show that CBM addition promotes generation of additional reducing ends in the insoluble substrate by cellulases. On the contrary, bovine serum albumin (BSA), widely used in prevention of a nonspecific protein binding, causes an increase in soluble reducing-end production, when applied jointly with cellulases. We demonstrate that binding of CBMs to cellulose is non-homogeneous, irreversible and leads to its amorphisation. Our results also reveal effects of CBM-promoted amorphogenesis on cellulose hydrolysis by cellulases. (AU)

• Processo FAPESP: 10/18773-8 - Clonagem molecular, expressão, purificação e caracterização estrutural da endoglucanase de Trichoderma harzianum visando o desenvolvimento de coquetéis enzimáticos para a produção de etanol lignocelulósico
• Beneficiário: Vanessa de Oliveira Arnoldi Pellegrini
• Modalidade de apoio: Bolsas no Brasil - Doutorado Direto
• Processo FAPESP: 15/13684-0 - Estudos estruturais e funcionais de enzimas que participam na síntese e degradação de carboidratos complexos
• Beneficiário: Igor Polikarpov
• Modalidade de apoio: Auxílio à Pesquisa - Temático