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Impact of protein blocking on enzymatic saccharification of bagasse from sugarcane clones
Authors:Rafaela I. S. Ladeira Ázar  Túlio Morgan  Márcio H. P. Barbosa  Valéria M. Guimarães  Eduardo Ximenes  Michael Ladisch
Affiliation:1. Laboratory of Renewable Resources Engineering, Department of Agricultural and Biological Engineering, Purdue University, West Lafayette, Indiana

Department of Biochemistry and Molecular Biology, Federal University of Viçosa, Viçosa, Minas Gerais, Brazil;2. Department of Biochemistry and Molecular Biology, Federal University of Viçosa, Viçosa, Minas Gerais, Brazil;3. Department of Crop Science, Federal University of Viçosa, Viçosa, Minas Gerais, Brazil;4. Laboratory of Renewable Resources Engineering, Department of Agricultural and Biological Engineering, Purdue University, West Lafayette, Indiana

Abstract: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.
Keywords:adsorption isotherms  bagasse clones  bovine serum albumin  enzymatic hydrolysis  lignin
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