A Comparative study on lipase enzyme immobilized on acid and glutaraldehyde functionalized multiwalled carbon nanotubes

Nanomaterials are being increasingly employed as support materials for enzyme immobilization owing to their biocompatibility and large surface area. Immobilization of lipase on multiwalled carbon nanotubes (MWCNT) has shown significant enhancement in the enzyme stability with respect to temperature...

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Main Authors:	Jameel, Ahmed Tariq, Arif, Muhammad Arif
Format:	Conference or Workshop Item
Language:	English
Published:	Thai Society for Biotechnology (TSB) & Asian Federation of Biotechnology (AFOB) 2017
Subjects:	TP155 Chemical engineering TP248.13 Biotechnology
Online Access:	http://irep.iium.edu.my/63480/ http://irep.iium.edu.my/63480/ http://irep.iium.edu.my/63480/1/Abstract%20book%20of%20ACB%202017_Online%209%20Aug%202017.pdf

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recordtype	eprints
spelling	iium-634802018-04-23T08:45:35Z http://irep.iium.edu.my/63480/ A Comparative study on lipase enzyme immobilized on acid and glutaraldehyde functionalized multiwalled carbon nanotubes Jameel, Ahmed Tariq Arif, Muhammad Arif TP155 Chemical engineering TP248.13 Biotechnology Nanomaterials are being increasingly employed as support materials for enzyme immobilization owing to their biocompatibility and large surface area. Immobilization of lipase on multiwalled carbon nanotubes (MWCNT) has shown significant enhancement in the enzyme stability with respect to temperature and pH variations. Functionalization of MWCNT results into cross linking of enzyme with the MWCNT. The present study focused on the comparative performance evaluation of the immobilized lipase on MWCNT functionalized using acid and glutaraldehyde, respectively. Acid treatment of MWCNT will cause lipase to physically adsorb on MWCNT while glutaraldehyde treatment will act as a cross linker and form a covalent bond between lipase and the functionalized MWCNT. Immobilization efficiency was assessed by comparing enzyme loading for the two differently functionalized MWCNTs. Enzyme loading is defined as the ratio of the enzyme that is attached to the MWCNT to the enzyme present in the original enzyme solution. Glutaraldehyde-MWCNT (GL-MWCNT) cross-linking showed 96% of loading efficiency while acid treatment showed 94% efficiency. The maximum enzyme activity on GA-MWCNT was obtained at 45°C and pH 7 while acid-MWCNT showed highest activity at 40°C and pH 8. Enzyme activity was higher for lipase immobilized on GA-MWCNT compared to acid-MWCNT possibly owing to greater enzyme loading in the former support. Immobilized enzyme showed higher relative activity compared to the free enzyme. Lipase on GA-MWCNT showed greater stability at higher pH and temperature compared to that of the acid-MWCNT. Further, lipase on GA-MWCNT exhibited almost 81% residual activity after 5 consecutive uses. In short, GA-MWCNT appears to be a better support material for lipase performance in terms of operational stability, enhanced activity and high residual activity upon multiple uses. Thai Society for Biotechnology (TSB) & Asian Federation of Biotechnology (AFOB) 2017-07-23 Conference or Workshop Item PeerReviewed application/pdf en http://irep.iium.edu.my/63480/1/Abstract%20book%20of%20ACB%202017_Online%209%20Aug%202017.pdf Jameel, Ahmed Tariq and Arif, Muhammad Arif (2017) A Comparative study on lipase enzyme immobilized on acid and glutaraldehyde functionalized multiwalled carbon nanotubes. In: The 13th Asian Congress on Biotechnology 2017 (ACB 2017) “Bioinnovation and Bioeconomy”, 23-27, July 2017, Pullman Khon Kaen Raja Orchid Hotel, Khon Kaen, Thailand. (Unpublished) http://www.acb2017thailand.org/
repository_type	Digital Repository
institution_category	Local University
institution	International Islamic University Malaysia
building	IIUM Repository
collection	Online Access
language	English
topic	TP155 Chemical engineering TP248.13 Biotechnology
spellingShingle	TP155 Chemical engineering TP248.13 Biotechnology Jameel, Ahmed Tariq Arif, Muhammad Arif A Comparative study on lipase enzyme immobilized on acid and glutaraldehyde functionalized multiwalled carbon nanotubes
description	Nanomaterials are being increasingly employed as support materials for enzyme immobilization owing to their biocompatibility and large surface area. Immobilization of lipase on multiwalled carbon nanotubes (MWCNT) has shown significant enhancement in the enzyme stability with respect to temperature and pH variations. Functionalization of MWCNT results into cross linking of enzyme with the MWCNT. The present study focused on the comparative performance evaluation of the immobilized lipase on MWCNT functionalized using acid and glutaraldehyde, respectively. Acid treatment of MWCNT will cause lipase to physically adsorb on MWCNT while glutaraldehyde treatment will act as a cross linker and form a covalent bond between lipase and the functionalized MWCNT. Immobilization efficiency was assessed by comparing enzyme loading for the two differently functionalized MWCNTs. Enzyme loading is defined as the ratio of the enzyme that is attached to the MWCNT to the enzyme present in the original enzyme solution. Glutaraldehyde-MWCNT (GL-MWCNT) cross-linking showed 96% of loading efficiency while acid treatment showed 94% efficiency. The maximum enzyme activity on GA-MWCNT was obtained at 45°C and pH 7 while acid-MWCNT showed highest activity at 40°C and pH 8. Enzyme activity was higher for lipase immobilized on GA-MWCNT compared to acid-MWCNT possibly owing to greater enzyme loading in the former support. Immobilized enzyme showed higher relative activity compared to the free enzyme. Lipase on GA-MWCNT showed greater stability at higher pH and temperature compared to that of the acid-MWCNT. Further, lipase on GA-MWCNT exhibited almost 81% residual activity after 5 consecutive uses. In short, GA-MWCNT appears to be a better support material for lipase performance in terms of operational stability, enhanced activity and high residual activity upon multiple uses.
format	Conference or Workshop Item
author	Jameel, Ahmed Tariq Arif, Muhammad Arif
author_facet	Jameel, Ahmed Tariq Arif, Muhammad Arif
author_sort	Jameel, Ahmed Tariq
title	A Comparative study on lipase enzyme immobilized on acid and glutaraldehyde functionalized multiwalled carbon nanotubes
title_short	A Comparative study on lipase enzyme immobilized on acid and glutaraldehyde functionalized multiwalled carbon nanotubes
title_full	A Comparative study on lipase enzyme immobilized on acid and glutaraldehyde functionalized multiwalled carbon nanotubes
title_fullStr	A Comparative study on lipase enzyme immobilized on acid and glutaraldehyde functionalized multiwalled carbon nanotubes
title_full_unstemmed	A Comparative study on lipase enzyme immobilized on acid and glutaraldehyde functionalized multiwalled carbon nanotubes
title_sort	comparative study on lipase enzyme immobilized on acid and glutaraldehyde functionalized multiwalled carbon nanotubes
publisher	Thai Society for Biotechnology (TSB) & Asian Federation of Biotechnology (AFOB)
publishDate	2017
url	http://irep.iium.edu.my/63480/ http://irep.iium.edu.my/63480/ http://irep.iium.edu.my/63480/1/Abstract%20book%20of%20ACB%202017_Online%209%20Aug%202017.pdf
first_indexed	2023-09-18T21:30:02Z
last_indexed	2023-09-18T21:30:02Z
_version_	1777412449331314688

A Comparative study on lipase enzyme immobilized on acid and glutaraldehyde functionalized multiwalled carbon nanotubes

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