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Immobilization of Cellulase on Zinc Oxide Deposited on Zeolite Pellets for Enzymatic Saccharification of Cellulose
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Metadata
Document Title
Immobilization of Cellulase on Zinc Oxide Deposited on Zeolite Pellets for Enzymatic Saccharification of Cellulose
Author
Eom T. Isanapong J. Kumnorkaew P. Songthanasak K. Pornwongthong P.
Affiliations
Department of Agro-Industrial Food and Environmental Technology Faculty of Applied Science King Mongkut抯 University of Technology North Bangkok Bangkok Thailand; Innovative Nanocoating Research Team National Nanotechnology Center National Science and Technology Development Agency Pathum Thani Thailand; Food and Agro-Industry Research Center King Mongkut抯 University of Technology North Bangkok Bangkok Thailand; Agritech and Innovation Center King Mongkut抯 University of Technology North Bangkok Techno Park Bangkok Thailand
Type
Conference Paper
Source Title
E3S Web of Conferences
ISSN
25550403
Year
2023
Volume
428
Open Access
All Open Access Gold Green
Publisher
EDP Sciences
DOI
10.1051/e3sconf/202342802003
Abstract
The consumption of fossil fuels to fulfill the global energy demand can cause global warming issues. Renewable energy i.e. bioethanol from lignocellulosic biomass is a promising source of alternative energy to fossil fuels. The conversion of lignocellulosic biomass into bioethanol requires the release of fermentable sugars during the saccharification process using cellulase. However the utilization of this enzyme on an industrial scale is not feasible due to its difficult separation instability and high cost. Here we present a method for cellulase immobilization on functionalized zinc oxide prepared from either zinc nitrate hexahydrate (ZnO(I)) or zinc acetate dihydrate (ZnO(II)) solutions on zeolite (ZEO) pellets. The immobilized cellulase on ZnO-ZEO structures was characterized by scanning electron microscopy X-ray diffraction spectroscopy and Fourier transform infrared spectroscopy. The immobilization efficiencies of immobilized cellulase either on ZnO(I)-ZEO or ZnO(II)-ZEO were determined as 58.17 ? 0.75% and 55.51 ? 0.81% respectively. The immobilized cellulase on ZnO-ZEO was capable of catalyzing microcrystalline cellulose breakdown releasing reducing sugars. The immobilized cellulase on these structures could be recycled up to four repetitive runs. Based on kinetic data both the Michaelis constants (Km) and maximum reaction velocity (Vmax) of the immobilized cellulase on the ZnO-ZEO structures were lower than those of free cellulase. This suggests that immobilized cellulase has a higher affinity toward the substrate but a lower reaction rate than the free enzyme. ? The Authors published by EDP Sciences.
Keyword
Biocatalysis | Enzymatic hydrolysis | Enzyme kinetics | Reusability
License
CC BY
Rights
Authors
Publication Source
Scopus