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Title: Impact of protein blocking on enzymatic saccharification of bagasse from sugarcane clones

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.

Authors:
 [1];  [2];  [2]; ORCiD logo [2];  [3]; ORCiD logo [3]
  1. Purdue Univ., West Lafayette, IN (United States). Lab. of Renewable Resources Engineering; Federal Univ. of Viçosa (Brazil)
  2. Federal Univ. of Viçosa (Brazil)
  3. Purdue Univ., West Lafayette, IN (United States). Lab. of Renewable Resources Engineering
Publication Date:
Research Org.:
Purdue Univ., West Lafayette, IN (United States)
Sponsoring Org.:
USDOE Office of Energy Efficiency and Renewable Energy (EERE)
OSTI Identifier:
1613510
Alternate Identifier(s):
OSTI ID: 1994399
Grant/Contract Number:  
EE0008256
Resource Type:
Accepted Manuscript
Journal Name:
Biotechnology and Bioengineering
Additional Journal Information:
Journal Volume: 116; Journal Issue: 7; Journal ID: ISSN 0006-3592
Publisher:
Wiley
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; Biotechnology & applied microbiology; adsorption isotherms; bagasse clones; bovine serum albumin; enzymatic hydrolysis; lignin

Citation Formats

Ázar, Rafaela I. S. Ladeira, Morgan, Túlio, Barbosa, Márcio H. P., Guimarães, Valéria M., Ximenes, Eduardo, and Ladisch, Michael. Impact of protein blocking on enzymatic saccharification of bagasse from sugarcane clones. United States: N. p., 2019. Web. doi:10.1002/bit.26962.
Ázar, Rafaela I. S. Ladeira, Morgan, Túlio, Barbosa, Márcio H. P., Guimarães, Valéria M., Ximenes, Eduardo, & Ladisch, Michael. Impact of protein blocking on enzymatic saccharification of bagasse from sugarcane clones. United States. https://doi.org/10.1002/bit.26962
Ázar, Rafaela I. S. Ladeira, Morgan, Túlio, Barbosa, Márcio H. P., Guimarães, Valéria M., Ximenes, Eduardo, and Ladisch, Michael. Thu . "Impact of protein blocking on enzymatic saccharification of bagasse from sugarcane clones". United States. https://doi.org/10.1002/bit.26962. https://www.osti.gov/servlets/purl/1613510.
@article{osti_1613510,
title = {Impact of protein blocking on enzymatic saccharification of bagasse from sugarcane clones},
author = {Ázar, Rafaela I. S. Ladeira and Morgan, Túlio and Barbosa, Márcio H. P. and Guimarães, Valéria M. and Ximenes, Eduardo and Ladisch, Michael},
abstractNote = {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.},
doi = {10.1002/bit.26962},
journal = {Biotechnology and Bioengineering},
number = 7,
volume = 116,
place = {United States},
year = {Thu Mar 21 00:00:00 EDT 2019},
month = {Thu Mar 21 00:00:00 EDT 2019}
}

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Works referencing / citing this record:

Effect of Lignin Content on Cellulolytic Saccharification of Liquid Hot Water Pretreated Sugarcane Bagasse
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