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:
-
- Purdue Univ., West Lafayette, IN (United States). Lab. of Renewable Resources Engineering; Federal Univ. of Viçosa (Brazil)
- Federal Univ. of Viçosa (Brazil)
- 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}
}
Web of Science
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Works referencing / citing this record:
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