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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

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

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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]
Total Authors: 9
[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
Total Affiliations: 6
Document type: Journal article
Source: Carbohydrate Polymers; v. 211, p. 57-68, MAY 1 2019.
Web of Science Citations: 4

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)

FAPESP's process: 10/18773-8 - Molecular cloning, expression, purification and structural characterization of endoglucanase from Trichoderma harzianum aiming the development of enzymatic blends for production of lignocellulosic ethanol
Grantee:Vanessa de Oliveira Arnoldi Pellegrini
Support type: Scholarships in Brazil - Doctorate (Direct)
FAPESP's process: 15/13684-0 - Structural and functional studies of enzymes that participate in complex carbohydrates synthesis and degradation
Grantee:Igor Polikarpov
Support type: Research Projects - Thematic Grants