Immobilization of laccase enzyme on magnetically-separable hierarchically-ordered mesocellular mesoporous silica

Multicopper oxidases, known as laccase, are a sustainable biocatalyst with efficient ability to degrade a wide range of compounds, environmentally friendly properties and promise major advances in a wide range of industries. However, the use of free laccase in industries often suffers problems, such...

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Main Author:	Ahmad Jafri, Norsyafiqah Amalina
Format:	Thesis
Language:	English
Published:	2022
Subjects:	TP Chemical technology
Online Access:	http://eprints.utm.my/102995/1/NorsyafiqahAmalinaMSChe2022.pdf
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spelling	my-utm-ep.1029952023-10-12T08:41:36Z Immobilization of laccase enzyme on magnetically-separable hierarchically-ordered mesocellular mesoporous silica 2022 Ahmad Jafri, Norsyafiqah Amalina TP Chemical technology Multicopper oxidases, known as laccase, are a sustainable biocatalyst with efficient ability to degrade a wide range of compounds, environmentally friendly properties and promise major advances in a wide range of industries. However, the use of free laccase in industries often suffers problems, such as instability, low recovery and low reusability of enzyme. Hence, laccase immobilization on a magneticallyseparable hierarchically-ordered mesocellular mesoporous silica (M-HMMS) as the support material was optimized and characterized. In this study, three different immobilization methods used were enzyme adsorption, entrapped-crosslinked enzyme and entrapped-crosslinked enzyme aggregate. The optimum parameters for laccase immobilization were at 5 hr of crosslinking time, 100 mM glutaraldehyde concentration, 1 mg/ml laccase concentration, 60 min time of precipitation with pH 4.5 and temperature of 20 C. This optimal condition contributed to 65.03 ± 4.31 % of laccase activity recovery and enhancement by 2.6 fold. The adsorption of laccase on M-HMMS obeyed the pseudo-second-order kinetic model. The optimized immobilized laccase was able to withstand high temperature (50 ??) and also oxidize 2, 2-azino-bis 3- ethylbenzothiazoline-6- sulfonic acid (ABTS) at a broad range of pH (pH 3.0 to pH 6.0) and temperature (20 to 70c) It also retained 63.72 ± 6.59 % of its initial activity after 8 repeated cycles of ABTS oxidation and 100 % of its activity after 30 days of storage at 4c in pH 4.5 buffer. In conclusion, the optimized immobilized laccase has potential as immobilized biocatalyst for the application of bioremediation and biotransformation of contaminant molecules in water. 2022 Thesis http://eprints.utm.my/102995/ http://eprints.utm.my/102995/1/NorsyafiqahAmalinaMSChe2022.pdf application/pdf en public http://dms.library.utm.my:8080/vital/access/manager/Repository/vital:150704 masters Universiti Teknologi Malaysia Faculty of Engineering - School of Chemical & Energy Engineering
institution	Universiti Teknologi Malaysia
collection	UTM Institutional Repository
language	English
topic	TP Chemical technology
spellingShingle	TP Chemical technology Ahmad Jafri, Norsyafiqah Amalina Immobilization of laccase enzyme on magnetically-separable hierarchically-ordered mesocellular mesoporous silica
description	Multicopper oxidases, known as laccase, are a sustainable biocatalyst with efficient ability to degrade a wide range of compounds, environmentally friendly properties and promise major advances in a wide range of industries. However, the use of free laccase in industries often suffers problems, such as instability, low recovery and low reusability of enzyme. Hence, laccase immobilization on a magneticallyseparable hierarchically-ordered mesocellular mesoporous silica (M-HMMS) as the support material was optimized and characterized. In this study, three different immobilization methods used were enzyme adsorption, entrapped-crosslinked enzyme and entrapped-crosslinked enzyme aggregate. The optimum parameters for laccase immobilization were at 5 hr of crosslinking time, 100 mM glutaraldehyde concentration, 1 mg/ml laccase concentration, 60 min time of precipitation with pH 4.5 and temperature of 20 C. This optimal condition contributed to 65.03 ± 4.31 % of laccase activity recovery and enhancement by 2.6 fold. The adsorption of laccase on M-HMMS obeyed the pseudo-second-order kinetic model. The optimized immobilized laccase was able to withstand high temperature (50 ??) and also oxidize 2, 2-azino-bis 3- ethylbenzothiazoline-6- sulfonic acid (ABTS) at a broad range of pH (pH 3.0 to pH 6.0) and temperature (20 to 70c) It also retained 63.72 ± 6.59 % of its initial activity after 8 repeated cycles of ABTS oxidation and 100 % of its activity after 30 days of storage at 4c in pH 4.5 buffer. In conclusion, the optimized immobilized laccase has potential as immobilized biocatalyst for the application of bioremediation and biotransformation of contaminant molecules in water.
format	Thesis
qualification_level	Master's degree
author	Ahmad Jafri, Norsyafiqah Amalina
author_facet	Ahmad Jafri, Norsyafiqah Amalina
author_sort	Ahmad Jafri, Norsyafiqah Amalina
title	Immobilization of laccase enzyme on magnetically-separable hierarchically-ordered mesocellular mesoporous silica
title_short	Immobilization of laccase enzyme on magnetically-separable hierarchically-ordered mesocellular mesoporous silica
title_full	Immobilization of laccase enzyme on magnetically-separable hierarchically-ordered mesocellular mesoporous silica
title_fullStr	Immobilization of laccase enzyme on magnetically-separable hierarchically-ordered mesocellular mesoporous silica
title_full_unstemmed	Immobilization of laccase enzyme on magnetically-separable hierarchically-ordered mesocellular mesoporous silica
title_sort	immobilization of laccase enzyme on magnetically-separable hierarchically-ordered mesocellular mesoporous silica
granting_institution	Universiti Teknologi Malaysia
granting_department	Faculty of Engineering - School of Chemical & Energy Engineering
publishDate	2022
url	http://eprints.utm.my/102995/1/NorsyafiqahAmalinaMSChe2022.pdf
_version_	1783729234163793920

Immobilization of laccase enzyme on magnetically-separable hierarchically-ordered mesocellular mesoporous silica

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