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The Immobilization Of Candida Rugosa Lipase On The Chitosan Beads

The immobilized enzyme is an important catalyst which used mainly to increase the rate of reaction. One of the methods to immobilize the enzyme is by covalent bonding. In the present research, Candida rugosa (C. rugosa) lipase was successfully immobilized by the method of covalent bonding onto act...

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Main Author: Mohd Romli, Muliati
Format: Monograph
Language:English
Published: Universiti Sains Malaysia 2018
Subjects:
T Technology
TP Chemical Technology
Online Access:http://eprints.usm.my/54093/1/The%20Immobilization%20Of%20Candida%20Rugosa%20Lipase%20On%20The%20Chitosan%20Beads_Muliati%20Mohd%20Romli_K4_2018.pdf
http://eprints.usm.my/54093/
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spelling my.usm.eprints.54093 http://eprints.usm.my/54093/ The Immobilization Of Candida Rugosa Lipase On The Chitosan Beads Mohd Romli, Muliati T Technology TP Chemical Technology The immobilized enzyme is an important catalyst which used mainly to increase the rate of reaction. One of the methods to immobilize the enzyme is by covalent bonding. In the present research, Candida rugosa (C. rugosa) lipase was successfully immobilized by the method of covalent bonding onto activated chitosan beads. The immobilization of lipase on the chitosan beads was confirmed by determining lipase activity during hydrolysis of a standard substance. The effect of lipase and glutaraldehyde (GA) concentrations on immobilization yield and activity yield were investigated. In general, the concentration of GA and lipase gave significant effect on immobilization yield and activity yield. As the GA concentration increase, the activity yield was decreased, while as the lipase concentration increase, the immobilization yield relatively decrease. The highest immobilization yield was 77.335 %, were achieved at 6 % of GA and 0.001 g/mL of C. rugosa lipase. After that, the highest activity was 50.3613 IU, where obtained at 2 % of GA and 0.010 g/mL of C. rugosa lipase. The optimization of immobilization process parameters was carried out via Respond Surface Method (RSM). It has been found that the most optimal condition for immobilization was at 4 % glutaraldehyde concentration and 0.005 g/mL of C. rugosa lipase which gave 65.14 % of immobilization yield and 32.84 IU of unit activity. The immobilized lipase was used repeatedly in the hydrolysis reaction. It was found that the immobilized enzyme was more stable and has the ability to be used multiple times. Therefore, immobilization of lipase onto activated chitosan support was feasible and it can be reused for 7 times. However, the activities reduce to 53.67 % after the 7th cycle. Universiti Sains Malaysia 2018-06-01 Monograph NonPeerReviewed application/pdf en http://eprints.usm.my/54093/1/The%20Immobilization%20Of%20Candida%20Rugosa%20Lipase%20On%20The%20Chitosan%20Beads_Muliati%20Mohd%20Romli_K4_2018.pdf Mohd Romli, Muliati (2018) The Immobilization Of Candida Rugosa Lipase On The Chitosan Beads. Project Report. Universiti Sains Malaysia, Pusat Pengajian Kejuruteraan Kimia. (Submitted)
institution Universiti Sains Malaysia
building Hamzah Sendut Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Sains Malaysia
content_source USM Institutional Repository
url_provider http://eprints.usm.my/
language English
topic T Technology
TP Chemical Technology
spellingShingle T Technology
TP Chemical Technology
Mohd Romli, Muliati
The Immobilization Of Candida Rugosa Lipase On The Chitosan Beads
description The immobilized enzyme is an important catalyst which used mainly to increase the rate of reaction. One of the methods to immobilize the enzyme is by covalent bonding. In the present research, Candida rugosa (C. rugosa) lipase was successfully immobilized by the method of covalent bonding onto activated chitosan beads. The immobilization of lipase on the chitosan beads was confirmed by determining lipase activity during hydrolysis of a standard substance. The effect of lipase and glutaraldehyde (GA) concentrations on immobilization yield and activity yield were investigated. In general, the concentration of GA and lipase gave significant effect on immobilization yield and activity yield. As the GA concentration increase, the activity yield was decreased, while as the lipase concentration increase, the immobilization yield relatively decrease. The highest immobilization yield was 77.335 %, were achieved at 6 % of GA and 0.001 g/mL of C. rugosa lipase. After that, the highest activity was 50.3613 IU, where obtained at 2 % of GA and 0.010 g/mL of C. rugosa lipase. The optimization of immobilization process parameters was carried out via Respond Surface Method (RSM). It has been found that the most optimal condition for immobilization was at 4 % glutaraldehyde concentration and 0.005 g/mL of C. rugosa lipase which gave 65.14 % of immobilization yield and 32.84 IU of unit activity. The immobilized lipase was used repeatedly in the hydrolysis reaction. It was found that the immobilized enzyme was more stable and has the ability to be used multiple times. Therefore, immobilization of lipase onto activated chitosan support was feasible and it can be reused for 7 times. However, the activities reduce to 53.67 % after the 7th cycle.
format Monograph
author Mohd Romli, Muliati
author_facet Mohd Romli, Muliati
author_sort Mohd Romli, Muliati
title The Immobilization Of Candida Rugosa Lipase On The Chitosan Beads
title_short The Immobilization Of Candida Rugosa Lipase On The Chitosan Beads
title_full The Immobilization Of Candida Rugosa Lipase On The Chitosan Beads
title_fullStr The Immobilization Of Candida Rugosa Lipase On The Chitosan Beads
title_full_unstemmed The Immobilization Of Candida Rugosa Lipase On The Chitosan Beads
title_sort immobilization of candida rugosa lipase on the chitosan beads
publisher Universiti Sains Malaysia
publishDate 2018
url http://eprints.usm.my/54093/1/The%20Immobilization%20Of%20Candida%20Rugosa%20Lipase%20On%20The%20Chitosan%20Beads_Muliati%20Mohd%20Romli_K4_2018.pdf
http://eprints.usm.my/54093/
_version_ 1743107783903936512
score 13.211869

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