Immobilization of lipase in calcium alginate beads for the study of butyl acetate synthesis / Mohd Zulkhairi Abdul Rahim

Immobilization of lipase in calcium alginate beads for the study of butyl acetate synthesis / Mohd Zulkhairi Abdul Rahim

Literature about lipase (EC 3.1.1.3) , immobilized enzyme, alginate and chitosan are presented in thi s thesis. Thi s study involved the use of free and immobilized Iipases to catalyse esterification reaction of short chain fatty acid and alcohol to produce short chain ester. Generally , it involved...

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Main Author: Abdul Rahim, Mohd Zulkhairi
Format: Thesis
Language:English
Published: 2006
Subjects:
Biochemistry
Online Access:https://ir.uitm.edu.my/id/eprint/27425/2/27425.pdf
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spelling my-uitm-ir.274252024-04-23T06:57:16Z Immobilization of lipase in calcium alginate beads for the study of butyl acetate synthesis / Mohd Zulkhairi Abdul Rahim 2006 Abdul Rahim, Mohd Zulkhairi Biochemistry Literature about lipase (EC 3.1.1.3) , immobilized enzyme, alginate and chitosan are presented in thi s thesis. Thi s study involved the use of free and immobilized Iipases to catalyse esterification reaction of short chain fatty acid and alcohol to produce short chain ester. Generally , it involved the optimization of conditions of esterification reaction of acetic acid and n-butanol and followed by comparison of properties of immobilized enzyme with those of free enzyme. Results showed that 14.3 mg lipase , 80 umol n-butanol , 160 umol acetic acid and 3.0 days reaction time at a temp erature of 40 DC were the optimum conditions for lipase - CAB in terms of enzyme loading , immobilized enzyme concentration, temperature, substrate concentration and reaction time respectively. Meanwhile, 0.8% w/v of chitosan solution was chosen for the stabilized calcium alginate beads. Results showed that product conversion increased by increasing the temperature up to 50 DC for Lipase CAB and Lipase - CCAB but not for free lipase. Thermal stability test showed that Lipase - CAB and Lipa se - CCAB remained stable against temperature up to 60 DC compared to free lipase which had the highest activity at 30°C. The studies of effects of n-buta nol concentrations showed that increased in concentration of n-butanol above 40 umol decreased the conversion of product for Lipase - CCAB and free lipase. Meanwhile, conversion of product was affected by increasing concentration of n-butan ol to 80flmol and above for Lipase - CAB . In the study of effect of acetic acid, it was found that increasing concentration of acetic acid abovel60 umol decreased the product conver sion for Lipase - CAB and free lipase. However , Lipase - CCAB was not affected by high concentration of acetic acid up to 200 umol, Kinetic param eters , Km & Vmax of immobilized lipases for n-butanol were lower in values when compared with Km & Vmax values for acetic acid . Results showed that there were no stati stically significant different specific activities among the three systems studied. Operational stability test was important for repeated applications in batch or in a continuous reactor. It was demon strated that the enzyme was still active for at least 5 cycle s. Thus it was proven that immobilized lipase and free lipase were able to catalyse synthesis of short chain esters under the condition s studied. Continuous proce sses studies showed immobilized lipase had potential for such synthes is but need further studies . Several recommendations for further studies have also been suggested. 2006 Thesis https://ir.uitm.edu.my/id/eprint/27425/ https://ir.uitm.edu.my/id/eprint/27425/2/27425.pdf text en public masters Universiti Teknologi MARA Faculty of Applied Sciences
institution Universiti Teknologi MARA
collection UiTM Institutional Repository
language English
topic Biochemistry
spellingShingle Biochemistry
Abdul Rahim, Mohd Zulkhairi
Immobilization of lipase in calcium alginate beads for the study of butyl acetate synthesis / Mohd Zulkhairi Abdul Rahim
description Literature about lipase (EC 3.1.1.3) , immobilized enzyme, alginate and chitosan are presented in thi s thesis. Thi s study involved the use of free and immobilized Iipases to catalyse esterification reaction of short chain fatty acid and alcohol to produce short chain ester. Generally , it involved the optimization of conditions of esterification reaction of acetic acid and n-butanol and followed by comparison of properties of immobilized enzyme with those of free enzyme. Results showed that 14.3 mg lipase , 80 umol n-butanol , 160 umol acetic acid and 3.0 days reaction time at a temp erature of 40 DC were the optimum conditions for lipase - CAB in terms of enzyme loading , immobilized enzyme concentration, temperature, substrate concentration and reaction time respectively. Meanwhile, 0.8% w/v of chitosan solution was chosen for the stabilized calcium alginate beads. Results showed that product conversion increased by increasing the temperature up to 50 DC for Lipase CAB and Lipase - CCAB but not for free lipase. Thermal stability test showed that Lipase - CAB and Lipa se - CCAB remained stable against temperature up to 60 DC compared to free lipase which had the highest activity at 30°C. The studies of effects of n-buta nol concentrations showed that increased in concentration of n-butanol above 40 umol decreased the conversion of product for Lipase - CCAB and free lipase. Meanwhile, conversion of product was affected by increasing concentration of n-butan ol to 80flmol and above for Lipase - CAB . In the study of effect of acetic acid, it was found that increasing concentration of acetic acid abovel60 umol decreased the product conver sion for Lipase - CAB and free lipase. However , Lipase - CCAB was not affected by high concentration of acetic acid up to 200 umol, Kinetic param eters , Km & Vmax of immobilized lipases for n-butanol were lower in values when compared with Km & Vmax values for acetic acid . Results showed that there were no stati stically significant different specific activities among the three systems studied. Operational stability test was important for repeated applications in batch or in a continuous reactor. It was demon strated that the enzyme was still active for at least 5 cycle s. Thus it was proven that immobilized lipase and free lipase were able to catalyse synthesis of short chain esters under the condition s studied. Continuous proce sses studies showed immobilized lipase had potential for such synthes is but need further studies . Several recommendations for further studies have also been suggested.
format Thesis
qualification_level Master's degree
author Abdul Rahim, Mohd Zulkhairi
author_facet Abdul Rahim, Mohd Zulkhairi
author_sort Abdul Rahim, Mohd Zulkhairi
title Immobilization of lipase in calcium alginate beads for the study of butyl acetate synthesis / Mohd Zulkhairi Abdul Rahim
title_short Immobilization of lipase in calcium alginate beads for the study of butyl acetate synthesis / Mohd Zulkhairi Abdul Rahim
title_full Immobilization of lipase in calcium alginate beads for the study of butyl acetate synthesis / Mohd Zulkhairi Abdul Rahim
title_fullStr Immobilization of lipase in calcium alginate beads for the study of butyl acetate synthesis / Mohd Zulkhairi Abdul Rahim
title_full_unstemmed Immobilization of lipase in calcium alginate beads for the study of butyl acetate synthesis / Mohd Zulkhairi Abdul Rahim
title_sort immobilization of lipase in calcium alginate beads for the study of butyl acetate synthesis / mohd zulkhairi abdul rahim
granting_institution Universiti Teknologi MARA
granting_department Faculty of Applied Sciences
publishDate 2006
url https://ir.uitm.edu.my/id/eprint/27425/2/27425.pdf
_version_ 1804889604492361728

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