Immobilization of lipase from Candida Rugosa on chitosan beads for transesterification reaction.

Immobilization of lipase from Candida Rugosa on chitosan beads for transesterification reaction.

The objective of this study was to evaluate the immobilization of lipase on a chitosan support by physical adsorption, aiming its application in transesterification reactions. Immobilization of lipase give several advantages such as improved stability, reuse, continuous operation and the possibility...

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Main Author: Hasrul Azmi, Said
Format: Undergraduates Project Papers
Language:English
Published: 2008
Subjects:
QP Physiology
Online Access:http://umpir.ump.edu.my/id/eprint/668/
http://umpir.ump.edu.my/id/eprint/668/1/Hasrul_Azmi_B._Said.pdf
id ump-668
recordtype eprints
spelling ump-6682015-03-03T06:04:56Z http://umpir.ump.edu.my/id/eprint/668/ Immobilization of lipase from Candida Rugosa on chitosan beads for transesterification reaction. Hasrul Azmi, Said QP Physiology The objective of this study was to evaluate the immobilization of lipase on a chitosan support by physical adsorption, aiming its application in transesterification reactions. Immobilization of lipase give several advantages such as improved stability, reuse, continuous operation and the possibility of better control of reactions. Chitosan offers several advantages as an enzyme immobilization carrier such as versatility of available physical forms (flakes, porous beads, gel, fiber and membrane), low biodegradability and easy handling. In this study, bead porous of chitosan was used for immobilizing lipase from a microbial source of Candida rugosa. Lipase was immobilized by physical adsorption on chitosan following a previously developed methodology by Carneiro da Chunca et al. (1999). The ability of immobilized lipase on chitosan beads to catalyze transesterification of cooking oil and methanol was investigated. The important parameters like reaction time and oil to methanol molar ratios were studied to indentify the comparison between free lipase and immobilized lipase on transesterification reaction. From the study it was found that maximum conversion of ester using immobilized lipase and free lipase were 72.25% and 76.5% obtained at the optimum conditions of 1:4 molar ratios and reaction time of 48 hour. Therefore, the conversion of ester for free lipase was higher than immobilized lipase. As a conclusion, the chitosan beads were appear as a suitable support for immobilized lipase on trasnesterification reaction even though the ester conversion was lower than free lipase. On the other hand, immobilized lipase was provided an important advantage such as easy separation from the product and has a high potential to reuse. 2008-05 Undergraduates Project Papers NonPeerReviewed application/pdf en http://umpir.ump.edu.my/id/eprint/668/1/Hasrul_Azmi_B._Said.pdf Hasrul Azmi, Said (2008) Immobilization of lipase from Candida Rugosa on chitosan beads for transesterification reaction. Faculty of Chemical & Natural Resources Engineering, Universiti Malaysia Pahang.
repository_type Digital Repository
institution_category Local University
institution Universiti Malaysia Pahang
building UMP Institutional Repository
collection Online Access
language English
topic QP Physiology
spellingShingle QP Physiology
Hasrul Azmi, Said
Immobilization of lipase from Candida Rugosa on chitosan beads for transesterification reaction.
description The objective of this study was to evaluate the immobilization of lipase on a chitosan support by physical adsorption, aiming its application in transesterification reactions. Immobilization of lipase give several advantages such as improved stability, reuse, continuous operation and the possibility of better control of reactions. Chitosan offers several advantages as an enzyme immobilization carrier such as versatility of available physical forms (flakes, porous beads, gel, fiber and membrane), low biodegradability and easy handling. In this study, bead porous of chitosan was used for immobilizing lipase from a microbial source of Candida rugosa. Lipase was immobilized by physical adsorption on chitosan following a previously developed methodology by Carneiro da Chunca et al. (1999). The ability of immobilized lipase on chitosan beads to catalyze transesterification of cooking oil and methanol was investigated. The important parameters like reaction time and oil to methanol molar ratios were studied to indentify the comparison between free lipase and immobilized lipase on transesterification reaction. From the study it was found that maximum conversion of ester using immobilized lipase and free lipase were 72.25% and 76.5% obtained at the optimum conditions of 1:4 molar ratios and reaction time of 48 hour. Therefore, the conversion of ester for free lipase was higher than immobilized lipase. As a conclusion, the chitosan beads were appear as a suitable support for immobilized lipase on trasnesterification reaction even though the ester conversion was lower than free lipase. On the other hand, immobilized lipase was provided an important advantage such as easy separation from the product and has a high potential to reuse.
format Undergraduates Project Papers
author Hasrul Azmi, Said
author_facet Hasrul Azmi, Said
author_sort Hasrul Azmi, Said
title Immobilization of lipase from Candida Rugosa on chitosan beads for transesterification reaction.
title_short Immobilization of lipase from Candida Rugosa on chitosan beads for transesterification reaction.
title_full Immobilization of lipase from Candida Rugosa on chitosan beads for transesterification reaction.
title_fullStr Immobilization of lipase from Candida Rugosa on chitosan beads for transesterification reaction.
title_full_unstemmed Immobilization of lipase from Candida Rugosa on chitosan beads for transesterification reaction.
title_sort immobilization of lipase from candida rugosa on chitosan beads for transesterification reaction.
publishDate 2008
url http://umpir.ump.edu.my/id/eprint/668/
http://umpir.ump.edu.my/id/eprint/668/1/Hasrul_Azmi_B._Said.pdf
first_indexed 2023-09-18T21:53:08Z
last_indexed 2023-09-18T21:53:08Z
_version_ 1777413902671282176

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