Deactivation of Cellulase at the Air-Liquid Interface Is the Main Cause of Incomplete Cellulose Conversion at Low Enzyme Loadings
Abstract
Amphiphilic additives such as bovine serum albumin (BSA) and Tween have been used to improve cellulose hydrolysis by cellulases. However, there has been a lack of clarity to explain their mechanism of action in enzymatic hydrolysis of pure or low-lignin cellulosic substrates. In this work, a commercial Trichoderma reesei enzyme preparation and the amphiphilic additives BSA and Tween 20 were applied for hydrolysis of pure Avicel cellulose. The results showed that these additives only had large efects on cellulose conversion at low enzyme to substrate ratios when the reaction fasks were shaken. Furthermore, changes in the air-liquid interfacial area profoundly afected cellulose conversion, but surfactants reduced or prevented cellulase deactivation at the air-liquid interface. Not shaking the fasks or adding low amounts of surfactant resulted in near theoretical cellulose conversion at low enzyme loadings given enough reaction time. At low enzyme loadings, hydrolysis of cellulose in lignocellulosic biomass with low lignin content sufered from enhanced enzyme deactivation at the air-liquid interface.
- Authors:
-
[1];
- Univ. of California, Riverside, CA (United States). Bourns College of Engineering. Dept. of Chemical and Environmental Engineering; Univ. of California, Riverside, CA (United States). Bourns College of Engineering. Center for Environmental Research and Technology; Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). BioEnergy Science Center (BESC)
- Univ. of California, Riverside, CA (United States). Bourns College of Engineering. Center for Environmental Research and Technology; Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). BioEnergy Science Center (BESC)
- Publication Date:
- Research Org.:
- Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC)
- OSTI Identifier:
- 1624377
- Grant/Contract Number:
- AC05-00OR22725
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Scientific Reports
- Additional Journal Information:
- Journal Volume: 8; Journal Issue: 1; Journal ID: ISSN 2045-2322
- Publisher:
- Nature Publishing Group
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 09 BIOMASS FUELS; Science & Technology - Other Topics
Citation Formats
Bhagia, Samarthya, Dhir, Rachna, Kumar, Rajeev, and Wyman, Charles E. Deactivation of Cellulase at the Air-Liquid Interface Is the Main Cause of Incomplete Cellulose Conversion at Low Enzyme Loadings. United States: N. p., 2018.
Web. doi:10.1038/s41598-018-19848-3.
Bhagia, Samarthya, Dhir, Rachna, Kumar, Rajeev, & Wyman, Charles E. Deactivation of Cellulase at the Air-Liquid Interface Is the Main Cause of Incomplete Cellulose Conversion at Low Enzyme Loadings. United States. https://doi.org/10.1038/s41598-018-19848-3
Bhagia, Samarthya, Dhir, Rachna, Kumar, Rajeev, and Wyman, Charles E. Mon .
"Deactivation of Cellulase at the Air-Liquid Interface Is the Main Cause of Incomplete Cellulose Conversion at Low Enzyme Loadings". United States. https://doi.org/10.1038/s41598-018-19848-3. https://www.osti.gov/servlets/purl/1624377.
@article{osti_1624377,
title = {Deactivation of Cellulase at the Air-Liquid Interface Is the Main Cause of Incomplete Cellulose Conversion at Low Enzyme Loadings},
author = {Bhagia, Samarthya and Dhir, Rachna and Kumar, Rajeev and Wyman, Charles E.},
abstractNote = {Amphiphilic additives such as bovine serum albumin (BSA) and Tween have been used to improve cellulose hydrolysis by cellulases. However, there has been a lack of clarity to explain their mechanism of action in enzymatic hydrolysis of pure or low-lignin cellulosic substrates. In this work, a commercial Trichoderma reesei enzyme preparation and the amphiphilic additives BSA and Tween 20 were applied for hydrolysis of pure Avicel cellulose. The results showed that these additives only had large efects on cellulose conversion at low enzyme to substrate ratios when the reaction fasks were shaken. Furthermore, changes in the air-liquid interfacial area profoundly afected cellulose conversion, but surfactants reduced or prevented cellulase deactivation at the air-liquid interface. Not shaking the fasks or adding low amounts of surfactant resulted in near theoretical cellulose conversion at low enzyme loadings given enough reaction time. At low enzyme loadings, hydrolysis of cellulose in lignocellulosic biomass with low lignin content sufered from enhanced enzyme deactivation at the air-liquid interface.},
doi = {10.1038/s41598-018-19848-3},
journal = {Scientific Reports},
number = 1,
volume = 8,
place = {United States},
year = {Mon Jan 22 00:00:00 EST 2018},
month = {Mon Jan 22 00:00:00 EST 2018}
}
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Figure 1: Effect of BSA at low and high cellulase loadings on Avicel cellulose conversion. Low enzyme loading curves show cellulose conversion for up to 17 days of enzymatic hydrolysis of Avicel (1% glucan loading) with 5 mg enzyme (Accellerase® 1500) (square) and 5 mg enzyme with co-addition of 5more »
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