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Impact of protein blocking on enzymatic saccharification of bagasse from sugarcane clones
Author(s) -
Ázar Rafaela I. S. Ladeira,
Morgan Túlio,
Barbosa Márcio H. P.,
Guimarães Valéria M.,
Ximenes Eduardo,
Ladisch Michael
Publication year - 2019
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.26962
Subject(s) - bagasse , cellulase , lignin , chemistry , hydrolysis , enzymatic hydrolysis , cellulose , glucan , food science , sugar , biochemistry , biomass (ecology) , lignocellulosic biomass , botany , microbiology and biotechnology , biology , organic chemistry , agronomy
Lignin plays an important functional and structural role in plants, but also contributes to the recalcitrance of lignocellulosic biomass to hydrolysis. This study addresses the influence of lignin in hydrolysis of sugarcane bagasse from conventional bred lines (UFV260 and UFV204) that were selected from 432 field‐grown clones. In addition to higher sugar production, bagasse clone UFV204 had a small, but statistically significant, lower insoluble lignin content compared with clone UFV260 (15.5% vs, 16.6%) and also exhibited a significantly higher cellulose conversion to glucose (81.3% vs. 63.3%) at a cellulase loading of 5 (filter paper unit) FPU/g of glucan or 3 FPU/g total solids for liquid hot water pretreated bagasse (200°C, 10 min). The enzyme loading was further decreased by 50% to 2.5 FPU/g glucan and resulted in a similar glucan conversion (88.5%) for clone UFV204 when the bagasse was preincubated with bovine serum albumin at pH 4.8 and nonproductive binding of cellulase components was blocked. Comparison of Langmuir adsorption isotherms and differential adsorption of the three major cellulolytic enzyme components endoglucanase, cellobiohydrolase, and β‐glucosidase help to explain differences due to lignin content.