Immbolization of lipase on multi-walled carbon nanotubes

Alkhatib, Ma'an and Salleh, Hamzah and Sultan, Anans M. (2008) Immbolization of lipase on multi-walled carbon nanotubes. In: 2008 International Conference on Environment (ICENV 2008), 15-17 December, 2008, G Hotel, Penang. (Unpublished)

PDF (Immobilization of lipase on multi-walled carbon nanotubes) - Accepted Version Restricted to Repository staff only Download (142kB) | Request a copy

Abstract

Immobilized enzymes, such as lipases, have diverse applications including chemical, fuel, pharmaceutical and food processing industries. In this study, commercially available lipase extracted from Aspergillus niger has been immobilized on (MWNTs). The enzyme was bound to carbon nanotubes by covalent bonding, in the presence of N-(3-dimethylaminopropyl)-N'-ethyl)-carbodiimide (EDC) as a coupling reagent. Carbon nanotubes were carboxylated by sonication in 1 M nitric acid prior to treatment with the coupling reagent. Native lipase showed an activity of 2.22 x 10-3 U, whereas, immobilized lipase demonstrated an activity of 0.335 x 10-3, retaining 55 % of the native activity given that only 27.4 % enzyme immobilization has been achieved. One unit is defined as 1nmol of p-nitrophenol released by the hydrolysis of the substrate 4-nitrophenyl palmitate (pNPP) per 1 ml per minute.

Item Type:	Conference or Workshop Item (Full Paper)
Additional Information:	5595/2613
Uncontrolled Keywords:	MWNTs; SWNTs; CNTs; EDC; pNPP
Subjects:	T Technology > TA Engineering (General). Civil engineering (General) > TA401 Materials of engineering and construction T Technology > TP Chemical technology > TP248.13 Biotechnology
Kulliyyahs/Centres/Divisions/Institutes (Can select more than one option. Press CONTROL button):	Kulliyyah of Engineering > Department of Biotechnology Engineering
Depositing User:	Dr. Ma'an Alkhatib
Date Deposited:	28 Oct 2011 11:52
Last Modified:	16 Nov 2011 22:20
URI:	http://irep.iium.edu.my/id/eprint/2613

Actions (login required)

View Item