TY - JOUR
T1 - Carbohydrate binding modules enhance cellulose enzymatic hydrolysis by increasing access of cellulases to the substrate
AU - Bernardes, Amanda
AU - Pellegrini, Vanessa
AU - Curtolo, F
AU - Camilo, César
AU - Mello, Bruno
AU - Johns, Marcus
AU - Scott, Janet
AU - Guimarães, Francisco
AU - Polikarpov, Igor
PY - 2019/5/1
Y1 - 2019/5/1
N2 - 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 non-specific 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.
AB - 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 non-specific 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.
U2 - 10.1016/j.carbpol.2019.01.108
DO - 10.1016/j.carbpol.2019.01.108
M3 - Article (Academic Journal)
C2 - 30824104
SN - 0144-8617
VL - 211
SP - 57
EP - 68
JO - Carbohydrate Polymers
JF - Carbohydrate Polymers
ER -