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Hydrolysis of ionic liquid杢reated substrate with an Iocasia fonsfrigidae strain SP3-1 endoglucanase
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Document Title
Hydrolysis of ionic liquid杢reated substrate with an Iocasia fonsfrigidae strain SP3-1 endoglucanase
Author
Heng S. Sutheeworapong S. Wangnai C. Champreda V. Kosugi A. Ratanakhanokchai K. Tachaapaikoon C. Ceballos R.M.
Affiliations
School of Bioresources and Technology King Mongkut抯 University of Technology Thonburi Bangkok 10150 Thailand; Department of Molecular and Cell Biology University of California Merced CA 95343 United States; Systems Biology and Bioinformatics Laboratory Pilot Plant Development and Training Institute King Mongkut抯 University of Technology Thonburi Bangkok 10150 Thailand; Pilot Plant Development and Training Institute King Mongkut抯 University of Technology Thonburi Bangkok Thailand; National Center for Genetic Engineering and Biotechnology 113 Thailand Science Park Paholyothin Road Klong Luang Pathumthani 12120 Thailand; Biological Resources and Post-Harvest Division Japan International Research Center for Agricultural Sciences Ibaraki Japan; Excellent Center of Enzyme Technology and Microbial Utilization Pilot Plant Development and Training Institute King Mongkut抯 University of Technology Thonburi Bangkok 10150 Thailand; Quantitative Systems Biology Program University of California Merced CA 95343 United States
Type
Article
Source Title
Applied Microbiology and Biotechnology
ISSN
1757598
Year
2024
Volume
108
Issue
1
Open Access
All Open Access Hybrid Gold Green
Publisher
Springer Science and Business Media Deutschland GmbH
DOI
10.1007/s00253-023-12918-1
Abstract
Abstract: Recently we reported the discovery of a novel endoglucanase of the glycoside hydrolase family 12 (GH12) designated IfCelS12A from the haloalkaliphilic anaerobic bacterium Iocasia fonsfrigidae strain SP3-1 which was isolated from a hypersaline pond in the Samut Sakhon province of Thailand (ca. 2017). IfCelS12A exhibits high substrate specificity on carboxymethyl cellulose and amorphous cellulose but low substrate specificity on b-1 3;1 4-glucan. Unlike some endoglucanases of the GH12 family IfCelS12A does not exhibit hydrolytic activity on crystalline cellulose (i.e. Avicel?). High-Pressure Liquid Chromatography (HPLC) and Thin Layer Chromatography (TLC) analyses of products resulting from IfCelS12-mediated hydrolysis indicate mode of action for this enzyme. Notably IfCelS12A preferentially hydrolyzes cellotetraoses cellopentaoses and cellohexaoses with negligible activity on cellobiose or cellotriose. Kinetic analysis with cellopentaose and barely b-d-glucan as cellulosic substrates were conducted. On cellopentaose IfCelS12A demonstrates a 16-fold increase in activity (KM = 0.27 mM; kcat = 0.36 s?1; kcat /KM = 1.34 mM?1 s?1) compared to the enzymatic hydrolysis of barley b-d-glucan (KM: 0.04 mM kcat: 0.51 s?1 kcat /KM = 0.08 mM?1 s?1). Moreover IfCelS12A enzymatic efficacy is stable in hypersaline sodium chlorids (NaCl) solutions (up to 10% NaCl). Specifically IfCel12A retains notable activity after 24 h at 2M NaCl (10% saline solution). IfCelS12A used as a cocktail component with other cellulolytic enzymes and in conjunction with mobile sequestration platform technology offers additional options for deconstruction of ionic liquid杙retreated cellulosic feedstock. Key points: � IfCelS12A from an anaerobic alkaliphile Iocasia fronsfrigidae shows salt tolerance � IfCelS12A in cocktails with other enzymes efficiently degrades cellulosic biomass � IfCelS12A used with mobile enzyme sequestration platforms enhances hydrolysis. ? 2024 The Author(s).
License
CC BY
Rights
Springer Nature
Publication Source
WOS