CO-immobilization of cellulase and xylanase on magnetically-separable hierarchically-ordered mesocellular mesoporous silica

Thesis (PhD. (Bioprocess Engineering))

Bibliographic Details
Main Author: Sulaiman, Nurul Jannah
Format: Thesis
Language:English
Published: Universiti Teknologi Malaysia 2023
Subjects:
Online Access:http://openscience.utm.my/handle/123456789/823
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author Sulaiman, Nurul Jannah
author_facet Sulaiman, Nurul Jannah
author_sort Sulaiman, Nurul Jannah
collection OpenScience
description Thesis (PhD. (Bioprocess Engineering))
first_indexed 2024-03-05T17:34:52Z
format Thesis
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institution Universiti Teknologi Malaysia - OpenScience
language English
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spelling oai:openscience.utm.my:123456789/8232023-11-19T11:00:22Z CO-immobilization of cellulase and xylanase on magnetically-separable hierarchically-ordered mesocellular mesoporous silica Sulaiman, Nurul Jannah Lignocellulose—Biodegradation Immobilized enzymes—Biotechnology Enzymes—Research Thesis (PhD. (Bioprocess Engineering)) Lignocellulosic biomass that exist abundantly in nature is a potential source for producing environmentally sustainable biobased chemicals. Lignocellulosic materials can be converted into fuels and value-added chemicals by the method of enzymatic hydrolysis using cellulase and xylanase enzymes. However, the use of free enzymes is hampered by the low storage stability, difficulty in recovery and non-reusability of the enzymes, which leads to the need for enzyme immobilization. Several inorganic carriers are potentially suitable for enzymatic immobilization, by means of several different techniques. Enzyme immobilization in magnetically-separable hierarchically-ordered mesocellular mesoporous silica (M-HMMS) is an alternative method for producing efficient biocatalyst. In this study, cellulase and xylanase were immobilized using three approaches: enzyme adsorption, enzyme adsorption and cross-linking and enzyme adsorption, precipitation and cross-linking (EAPC). The best precipitant, cross-linker and immobilization method for cellulase and xylanase co-immobilization were tert-butanol, glutaraldehyde and EAPC, respectively. The optimum cellulase and xylanase activity retention were achieved using 2 mL of enzymes, 1 mg: 0.15 mL of magnetic silica-to-enzyme ratio, adsorption temperature of 26 ºC, adsorption time of 40 min, adsorption agitation rate of 162 rpm, 1:11 mL volume of enzyme-to-precipitant ratio, 0.05 % v/v of glutaraldehyde concentration, cross-linking temperature of 37 ºC, 2 hours of cross-linking time and cross-linking agitation rate of 300 rpm. The biocatalysts prepared under optimized condition retained the activity more than 90% with improved storage stability (above 60 % after 14 days). Adsorption study showed that the pseudo-second-order kinetic model and Kolmogorov-Erofeev-Kazeeva-Avrami-Mampel model were the best models to represent the kinetic adsorption process of cellulase and xylanase on M-HMMS. The sorption process was found to be physisorption for cellulase and chemisorption for xylanase, as predicted by the activation energies. The results suggest that co-immobilized cellulase and xylanase in M-HMMS is a promising biocatalyst. Faculty of Engineering - School of Chemical & Energy Engineering 2023-11-19T02:28:20Z 2023-11-19T02:28:20Z 2020 Thesis Dataset http://openscience.utm.my/handle/123456789/823 en application/pdf application/pdf application/pdf application/pdf application/pdf application/pdf Universiti Teknologi Malaysia
spellingShingle Lignocellulose—Biodegradation
Immobilized enzymes—Biotechnology
Enzymes—Research
Sulaiman, Nurul Jannah
CO-immobilization of cellulase and xylanase on magnetically-separable hierarchically-ordered mesocellular mesoporous silica
title CO-immobilization of cellulase and xylanase on magnetically-separable hierarchically-ordered mesocellular mesoporous silica
title_full CO-immobilization of cellulase and xylanase on magnetically-separable hierarchically-ordered mesocellular mesoporous silica
title_fullStr CO-immobilization of cellulase and xylanase on magnetically-separable hierarchically-ordered mesocellular mesoporous silica
title_full_unstemmed CO-immobilization of cellulase and xylanase on magnetically-separable hierarchically-ordered mesocellular mesoporous silica
title_short CO-immobilization of cellulase and xylanase on magnetically-separable hierarchically-ordered mesocellular mesoporous silica
title_sort co immobilization of cellulase and xylanase on magnetically separable hierarchically ordered mesocellular mesoporous silica
topic Lignocellulose—Biodegradation
Immobilized enzymes—Biotechnology
Enzymes—Research
url http://openscience.utm.my/handle/123456789/823
work_keys_str_mv AT sulaimannuruljannah coimmobilizationofcellulaseandxylanaseonmagneticallyseparablehierarchicallyorderedmesocellularmesoporoussilica