Impacts of cellulase deactivation at the moving air–liquid interface on cellulose conversions at low enzyme loadings
Abstract
Background: We recently confirmed that the deactivation of T. reesei cellulases at the air–liquid interface reduces microcrystalline cellulose conversion at low enzyme loadings in shaken flasks. It is one of the main causes for lowering of cellulose conversions at low enzyme loadings. However, supplementing cellulases with small quantities of surface-active additives in shaken flasks can increase cellulose conversions at low enzyme loadings. It was also shown that cellulose conversions at low enzyme loadings can be increased in unshaken flasks if the reactions are carried for a longer time. This study further explores these recent findings to better understand the impact of air–liquid interfacial phenomena on enzymatic hydrolysis of cellulose contained in Avicel, Sigmacell, α-cellulose, cotton linters, and filter paper. The impacts of solids and enzyme loadings, supplementation with nonionic surfactant Tween 20 and xylanases, and application of different types of mixing and reactor designs on cellulose hydrolysis were also evaluated.Results: Avicel cellulose conversions at high solid loading were more than doubled by minimizing loss of cellulases to the air–liquid interface. Maximum cellulose conversions were high for surface-active supplemented shaken flasks or unshaken flasks because of low cellulase deactivation at the air–liquid interface. The nonionic surfactant Tween 20 was unable tomore »
- Authors:
-
[2];
- Univ. of California, Riverside, CA (United States). Bourns College of Engineering, Center for Environmental Research and Technology (CE‑CERT) and Center for Environmental Research and Technology (CE‑CERT); 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 (CE‑CERT) and Center for Environmental Research and Technology (CE‑CERT); Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). BioEnergy Science Center (BESC) and Center for Bioenergy Innovation (CBI)
- Univ. of California, Riverside, CA (United States). Bourns College of Engineering, Center for Environmental Research and Technology (CE‑CERT); Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). BioEnergy Science Center (BESC) and Center for Bioenergy Innovation (CBI)
- Publication Date:
- Research Org.:
- Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)
- Sponsoring Org.:
- USDOE
- OSTI Identifier:
- 1511911
- Grant/Contract Number:
- AC05-00OR22725
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Biotechnology for Biofuels
- Additional Journal Information:
- Journal Volume: 12; Journal Issue: 1; Journal ID: ISSN 1754-6834
- Publisher:
- BioMed Central
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; Cellulose; Cellulase; Deactivation; Hydrolysis; Air–liquid interface; Gas–liquid interface
Citation Formats
Bhagia, Samarthya, Wyman, Charles E., and Kumar, Rajeev. Impacts of cellulase deactivation at the moving air–liquid interface on cellulose conversions at low enzyme loadings. United States: N. p., 2019.
Web. doi:10.1186/s13068-019-1439-2.
Bhagia, Samarthya, Wyman, Charles E., & Kumar, Rajeev. Impacts of cellulase deactivation at the moving air–liquid interface on cellulose conversions at low enzyme loadings. United States. https://doi.org/10.1186/s13068-019-1439-2
Bhagia, Samarthya, Wyman, Charles E., and Kumar, Rajeev. Tue .
"Impacts of cellulase deactivation at the moving air–liquid interface on cellulose conversions at low enzyme loadings". United States. https://doi.org/10.1186/s13068-019-1439-2. https://www.osti.gov/servlets/purl/1511911.
@article{osti_1511911,
title = {Impacts of cellulase deactivation at the moving air–liquid interface on cellulose conversions at low enzyme loadings},
author = {Bhagia, Samarthya and Wyman, Charles E. and Kumar, Rajeev},
abstractNote = {Background: We recently confirmed that the deactivation of T. reesei cellulases at the air–liquid interface reduces microcrystalline cellulose conversion at low enzyme loadings in shaken flasks. It is one of the main causes for lowering of cellulose conversions at low enzyme loadings. However, supplementing cellulases with small quantities of surface-active additives in shaken flasks can increase cellulose conversions at low enzyme loadings. It was also shown that cellulose conversions at low enzyme loadings can be increased in unshaken flasks if the reactions are carried for a longer time. This study further explores these recent findings to better understand the impact of air–liquid interfacial phenomena on enzymatic hydrolysis of cellulose contained in Avicel, Sigmacell, α-cellulose, cotton linters, and filter paper. The impacts of solids and enzyme loadings, supplementation with nonionic surfactant Tween 20 and xylanases, and application of different types of mixing and reactor designs on cellulose hydrolysis were also evaluated.Results: Avicel cellulose conversions at high solid loading were more than doubled by minimizing loss of cellulases to the air–liquid interface. Maximum cellulose conversions were high for surface-active supplemented shaken flasks or unshaken flasks because of low cellulase deactivation at the air–liquid interface. The nonionic surfactant Tween 20 was unable to completely prevent cellulase deactivation in shaken flasks and only reduced cellulose conversions at unreasonably high concentrations.Conclusions: High dynamic interfacial areas created through baffles in reactor vessels, low volumes in high-capacity vessels, or high shaking speeds severely limited cellulose conversions at low enzyme loadings. Precipitation of cellulases due to aggregation at the air–liquid interface caused their continuous deactivation in shaken flasks and severely limited solubilization of cellulose.},
doi = {10.1186/s13068-019-1439-2},
journal = {Biotechnology for Biofuels},
number = 1,
volume = 12,
place = {United States},
year = {Tue Apr 23 00:00:00 EDT 2019},
month = {Tue Apr 23 00:00:00 EDT 2019}
}
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Figures / Tables:
Fig. 1: Effects of surfactant supplementation and shaking on conversions of cellulosic substrates at low enzyme loading. Cellulose conversions are reported after 5, 11, and 17 days of enzymatic hydrolysis of model cellulosic substrates at 1% glucan loadings using 5 mg cellulase protein ( Accellerase® 1500) per g glucan inmore »
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