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Title: Hydrolysis‐determining substrate characteristics in liquid hot water pretreated hardwood

Abstract

ABSTRACT Fundamental characterization of pretreated hardwood and its interactions with cellulolytic enzymes has confirmed that a pathway exists for dramatically reducing the loading of cellulase required for hydrolysis of pretreated biomass. We demonstrate that addition of protein effecting a seven‐fold decrease in the specific activity of cellulases enables a ten‐fold reduction in enzyme loading while maintaining a high level of cellulose hydrolysis in pretreated hardwood. While use of protein and other additives that adsorb on lignin have been reported previously, the current work demonstrates the effect in a dramatic manner and brings the rationale for this change into clear focus. The key to this result is recognizing and mitigating the pretreatment conundrum where increasingly severe pretreatment conditions enhance accessibility of the enzymes not only to cellulose, but also to lignin. The lignin adsorbs enzyme protein causing loss of cellulase activity. More enzyme, added to compensate for this lost activity, results in a higher cellulase loading. The addition of a different protein, such as BSA, prevents cellulase adsorption on lignin and enables the enzyme itself to better target its glucan substrate. This effect dramatically reduces the amount of cellulase for a given level of conversion with enzyme loadings of 15 FPUmore » and 1.3 FPU/g solids both achieving 80% conversion. The understanding of this phenomenon reinvigorates motivation for the search for other approaches that prevent cellulase adsorption on lignin in order to achieve high glucose yields at low enzyme loadings for pretreated lignocellulose. Biotechnol. Bioeng. 2015;112: 677–687. © 2014 Wiley Periodicals, Inc.« less

Authors:
 [1];  [1];  [1];  [2]
  1. Laboratory of Renewable Resources Engineering Purdue University West Lafayette Indiana, Department of Agricultural and Biological Engineering Purdue University West Lafayette Indiana
  2. Laboratory of Renewable Resources Engineering Purdue University West Lafayette Indiana, Department of Agricultural and Biological Engineering Purdue University West Lafayette Indiana, Weldon School of Biomedical Engineering Purdue University West Lafayette Indiana 47907
Publication Date:
Sponsoring Org.:
USDOE
OSTI Identifier:
1400500
Grant/Contract Number:  
DE‐AC36‐99GO10337; DOE DE‐FG02‐06ER06‐03; GO12O26‐174; DE‐FG02‐06ER64301; GO18103
Resource Type:
Publisher's Accepted Manuscript
Journal Name:
Biotechnology and Bioengineering
Additional Journal Information:
Journal Name: Biotechnology and Bioengineering Journal Volume: 112 Journal Issue: 4; Journal ID: ISSN 0006-3592
Publisher:
Wiley Blackwell (John Wiley & Sons)
Country of Publication:
United States
Language:
English

Citation Formats

Kim, Youngmi, Kreke, Thomas, Ko, Ja Kyong, and Ladisch, Michael R. Hydrolysis‐determining substrate characteristics in liquid hot water pretreated hardwood. United States: N. p., 2015. Web. doi:10.1002/bit.25465.
Kim, Youngmi, Kreke, Thomas, Ko, Ja Kyong, & Ladisch, Michael R. Hydrolysis‐determining substrate characteristics in liquid hot water pretreated hardwood. United States. https://doi.org/10.1002/bit.25465
Kim, Youngmi, Kreke, Thomas, Ko, Ja Kyong, and Ladisch, Michael R. Fri . "Hydrolysis‐determining substrate characteristics in liquid hot water pretreated hardwood". United States. https://doi.org/10.1002/bit.25465.
@article{osti_1400500,
title = {Hydrolysis‐determining substrate characteristics in liquid hot water pretreated hardwood},
author = {Kim, Youngmi and Kreke, Thomas and Ko, Ja Kyong and Ladisch, Michael R.},
abstractNote = {ABSTRACT Fundamental characterization of pretreated hardwood and its interactions with cellulolytic enzymes has confirmed that a pathway exists for dramatically reducing the loading of cellulase required for hydrolysis of pretreated biomass. We demonstrate that addition of protein effecting a seven‐fold decrease in the specific activity of cellulases enables a ten‐fold reduction in enzyme loading while maintaining a high level of cellulose hydrolysis in pretreated hardwood. While use of protein and other additives that adsorb on lignin have been reported previously, the current work demonstrates the effect in a dramatic manner and brings the rationale for this change into clear focus. The key to this result is recognizing and mitigating the pretreatment conundrum where increasingly severe pretreatment conditions enhance accessibility of the enzymes not only to cellulose, but also to lignin. The lignin adsorbs enzyme protein causing loss of cellulase activity. More enzyme, added to compensate for this lost activity, results in a higher cellulase loading. The addition of a different protein, such as BSA, prevents cellulase adsorption on lignin and enables the enzyme itself to better target its glucan substrate. This effect dramatically reduces the amount of cellulase for a given level of conversion with enzyme loadings of 15 FPU and 1.3 FPU/g solids both achieving 80% conversion. The understanding of this phenomenon reinvigorates motivation for the search for other approaches that prevent cellulase adsorption on lignin in order to achieve high glucose yields at low enzyme loadings for pretreated lignocellulose. Biotechnol. Bioeng. 2015;112: 677–687. © 2014 Wiley Periodicals, Inc.},
doi = {10.1002/bit.25465},
journal = {Biotechnology and Bioengineering},
number = 4,
volume = 112,
place = {United States},
year = {Fri Jan 02 00:00:00 EST 2015},
month = {Fri Jan 02 00:00:00 EST 2015}
}

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Free Publicly Available Full Text
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https://doi.org/10.1002/bit.25465

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