Immobilization of cellulases enzyme on Carbon Nanotubes (CNTs) for cellulosic compounds degradation
The fast growing palm oil industry in Malaysia generates, amongst other wastes, Empty Fruit Bunch (EFB) which consists of cellulosic materials. It is one of the major sources of Greenhouse Gases (GHG). However, the bioconversion of cellulosic materials in EFB, a renewable biomass, to valuable pr...
Main Authors: | , , |
---|---|
Format: | Conference or Workshop Item |
Language: | English |
Published: |
2010
|
Subjects: | |
Online Access: | http://irep.iium.edu.my/23101/ http://irep.iium.edu.my/23101/ http://irep.iium.edu.my/23101/1/pp41.pdf |
id |
iium-23101 |
---|---|
recordtype |
eprints |
spelling |
iium-231012013-06-19T01:39:46Z http://irep.iium.edu.my/23101/ Immobilization of cellulases enzyme on Carbon Nanotubes (CNTs) for cellulosic compounds degradation Al-Khatib, Ma An Fahmi Rashid Alam, Md. Zahangir Mohammed Abd, Rasha TA401 Materials of engineering and construction The fast growing palm oil industry in Malaysia generates, amongst other wastes, Empty Fruit Bunch (EFB) which consists of cellulosic materials. It is one of the major sources of Greenhouse Gases (GHG). However, the bioconversion of cellulosic materials in EFB, a renewable biomass, to valuable products will be the solution to the disposal problem and hence minimize the pollution. The bioconversion of cellulosic materials is carried out by using cellulase enzyme, which itself was extracted from sludge, immobilized on functionalized carbon nanotubes (CNTs) in the presence of coupling reagent. The process parameters such as reaction temperature, reaction time, pH, and amount of enzyme, CNTs dosage and EDC were optimized by using design expert software. The morphology and the structure of CNTs were characterized by Field Emission Scanning Electron Microscopy (FSEM) and Fourier Transform Infrared Absorption Spectroscopic (FTIR). Firstly, carbon nanotubes were functionalized by acidic treatment. Then, the cellulase enzyme is immobilized on the functionalized (CNTs) in a solution of Nhydroxysuccinimide (NHS) and 1-ethyl-3-(3-dimethylamino propyl)-carbodiimide hydrochloride (EDC). The amount of enzyme attached on (CNTs) will be measured through UV spectrometer to determine the cellulases catalytic activity after immobilization and compare it with the free enzyme. Finally, the immobilized enzyme will be tested in the degradation of cellulosic material of empty fruit bunch (EFB) from palm oil mill effluent. 2010 Conference or Workshop Item PeerReviewed application/pdf en http://irep.iium.edu.my/23101/1/pp41.pdf Al-Khatib, Ma An Fahmi Rashid and Alam, Md. Zahangir and Mohammed Abd, Rasha (2010) Immobilization of cellulases enzyme on Carbon Nanotubes (CNTs) for cellulosic compounds degradation. In: IIUM Research, Innovation & Invention Exhibition (IRIIE 2010), 26 - 27 January 2010, Kuala Lumpur. http://www.iium.edu.my/irie/10/ |
repository_type |
Digital Repository |
institution_category |
Local University |
institution |
International Islamic University Malaysia |
building |
IIUM Repository |
collection |
Online Access |
language |
English |
topic |
TA401 Materials of engineering and construction |
spellingShingle |
TA401 Materials of engineering and construction Al-Khatib, Ma An Fahmi Rashid Alam, Md. Zahangir Mohammed Abd, Rasha Immobilization of cellulases enzyme on Carbon Nanotubes (CNTs) for cellulosic compounds degradation |
description |
The fast growing palm oil industry in Malaysia generates, amongst other wastes, Empty Fruit Bunch
(EFB) which consists of cellulosic materials. It is one of the major sources of Greenhouse Gases (GHG).
However, the bioconversion of cellulosic materials in EFB, a renewable biomass, to valuable products
will be the solution to the disposal problem and hence minimize the pollution. The bioconversion of
cellulosic materials is carried out by using cellulase enzyme, which itself was extracted from sludge,
immobilized on functionalized carbon nanotubes (CNTs) in the presence of coupling reagent. The process
parameters such as reaction temperature, reaction time, pH, and amount of enzyme, CNTs dosage and
EDC were optimized by using design expert software. The morphology and the structure of CNTs were
characterized by Field Emission Scanning Electron Microscopy (FSEM) and Fourier Transform Infrared
Absorption Spectroscopic (FTIR). Firstly, carbon nanotubes were functionalized by acidic treatment.
Then, the cellulase enzyme is immobilized on the functionalized (CNTs) in a solution of Nhydroxysuccinimide (NHS) and 1-ethyl-3-(3-dimethylamino propyl)-carbodiimide hydrochloride (EDC).
The amount of enzyme attached on (CNTs) will be measured through UV spectrometer to determine the
cellulases catalytic activity after immobilization and compare it with the free enzyme. Finally, the
immobilized enzyme will be tested in the degradation of cellulosic material of empty fruit bunch (EFB)
from palm oil mill effluent. |
format |
Conference or Workshop Item |
author |
Al-Khatib, Ma An Fahmi Rashid Alam, Md. Zahangir Mohammed Abd, Rasha |
author_facet |
Al-Khatib, Ma An Fahmi Rashid Alam, Md. Zahangir Mohammed Abd, Rasha |
author_sort |
Al-Khatib, Ma An Fahmi Rashid |
title |
Immobilization of cellulases enzyme on Carbon Nanotubes (CNTs) for cellulosic compounds degradation |
title_short |
Immobilization of cellulases enzyme on Carbon Nanotubes (CNTs) for cellulosic compounds degradation |
title_full |
Immobilization of cellulases enzyme on Carbon Nanotubes (CNTs) for cellulosic compounds degradation |
title_fullStr |
Immobilization of cellulases enzyme on Carbon Nanotubes (CNTs) for cellulosic compounds degradation |
title_full_unstemmed |
Immobilization of cellulases enzyme on Carbon Nanotubes (CNTs) for cellulosic compounds degradation |
title_sort |
immobilization of cellulases enzyme on carbon nanotubes (cnts) for cellulosic compounds degradation |
publishDate |
2010 |
url |
http://irep.iium.edu.my/23101/ http://irep.iium.edu.my/23101/ http://irep.iium.edu.my/23101/1/pp41.pdf |
first_indexed |
2023-09-18T20:35:01Z |
last_indexed |
2023-09-18T20:35:01Z |
_version_ |
1777408987897004032 |