Lipase-catalyzed preparation of galactose oleate ester in ionic liquid

Lipase-catalyzed preparation of galactose oleate ester was performed in 1-butyl-3-methylimidazolium tetrafluoroborate ([Bmim][BF4]) ionic liquid with the addition of dimethylsulfoxide (DMSO) as a solubilizing agent and co-solvent, and Lipozyme RM IM (lipase from Rhizomucor miehei immobilized on macr...

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Main Author:	Mohd Saupi, Hanim Salami
Format:	Thesis
Language:	English
Published:	2012
Subjects:	Molecular biology - Research Lipase
Online Access:	http://psasir.upm.edu.my/id/eprint/67129/1/FS%202012%2096%20IR.pdf
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id	my-upm-ir.67129
record_format	uketd_dc
spelling	my-upm-ir.671292019-02-20T07:17:03Z Lipase-catalyzed preparation of galactose oleate ester in ionic liquid 2012-10 Mohd Saupi, Hanim Salami Lipase-catalyzed preparation of galactose oleate ester was performed in 1-butyl-3-methylimidazolium tetrafluoroborate ([Bmim][BF4]) ionic liquid with the addition of dimethylsulfoxide (DMSO) as a solubilizing agent and co-solvent, and Lipozyme RM IM (lipase from Rhizomucor miehei immobilized on macroporous anion exchange resin) as the biocatalyst. Galactose oleate ester was purified and characterized by thin layer chromatography (TLC), fourier transform-infrared spectroscopy (FT-IR), high performance liquid chromatography (HPLC), direct injection-mass spectrometry (DI-MS), liquid chromatography-mass spectrometry (LC-MS) and nuclear magnetic resonance (NMR). Optimal preparation conditions with a high conversion rate (87%) was obtained in DMSO:[Bmim][BF4] (1:20, v:v) with 2% (w/w) Lipozyme RM IM loaded for 2 h, at 60C, with a stirring speed of 300 rpm and a molar ratio of galactose to oleic acid of 1:3. The formation of galactose oleate ester was evaluated through kinetic study using Michaelis-Menten kinetic model. The Ping-Pong Bi-Bi mechanism with one substrate inhibition was adopted as it best explained the experimental findings. The kinetic results showed the Km values (galactose = 0.02905 mmol/mL.mg and oleic acid = 0.00025 mmol/mL.mg). The low Michaelis constant values showed that the Lipozyme RM IM has higher affinity towards both substrates. The overall results on the physicochemical studies such as hydrophile lipophile balance (HLB) value, physical state, refractive index and surface tension illustrated that the ester possess suitability for industrial application as emulsifiers and surfactant. Molecular biology - Research Lipase 2012-10 Thesis http://psasir.upm.edu.my/id/eprint/67129/ http://psasir.upm.edu.my/id/eprint/67129/1/FS%202012%2096%20IR.pdf text en public masters Universiti Putra Malaysia Molecular biology - Research Lipase
institution	Universiti Putra Malaysia
collection	PSAS Institutional Repository
language	English
topic	Molecular biology - Research Lipase
spellingShingle	Molecular biology - Research Lipase Mohd Saupi, Hanim Salami Lipase-catalyzed preparation of galactose oleate ester in ionic liquid
description	Lipase-catalyzed preparation of galactose oleate ester was performed in 1-butyl-3-methylimidazolium tetrafluoroborate ([Bmim][BF4]) ionic liquid with the addition of dimethylsulfoxide (DMSO) as a solubilizing agent and co-solvent, and Lipozyme RM IM (lipase from Rhizomucor miehei immobilized on macroporous anion exchange resin) as the biocatalyst. Galactose oleate ester was purified and characterized by thin layer chromatography (TLC), fourier transform-infrared spectroscopy (FT-IR), high performance liquid chromatography (HPLC), direct injection-mass spectrometry (DI-MS), liquid chromatography-mass spectrometry (LC-MS) and nuclear magnetic resonance (NMR). Optimal preparation conditions with a high conversion rate (87%) was obtained in DMSO:[Bmim][BF4] (1:20, v:v) with 2% (w/w) Lipozyme RM IM loaded for 2 h, at 60C, with a stirring speed of 300 rpm and a molar ratio of galactose to oleic acid of 1:3. The formation of galactose oleate ester was evaluated through kinetic study using Michaelis-Menten kinetic model. The Ping-Pong Bi-Bi mechanism with one substrate inhibition was adopted as it best explained the experimental findings. The kinetic results showed the Km values (galactose = 0.02905 mmol/mL.mg and oleic acid = 0.00025 mmol/mL.mg). The low Michaelis constant values showed that the Lipozyme RM IM has higher affinity towards both substrates. The overall results on the physicochemical studies such as hydrophile lipophile balance (HLB) value, physical state, refractive index and surface tension illustrated that the ester possess suitability for industrial application as emulsifiers and surfactant.
format	Thesis
qualification_level	Master's degree
author	Mohd Saupi, Hanim Salami
author_facet	Mohd Saupi, Hanim Salami
author_sort	Mohd Saupi, Hanim Salami
title	Lipase-catalyzed preparation of galactose oleate ester in ionic liquid
title_short	Lipase-catalyzed preparation of galactose oleate ester in ionic liquid
title_full	Lipase-catalyzed preparation of galactose oleate ester in ionic liquid
title_fullStr	Lipase-catalyzed preparation of galactose oleate ester in ionic liquid
title_full_unstemmed	Lipase-catalyzed preparation of galactose oleate ester in ionic liquid
title_sort	lipase-catalyzed preparation of galactose oleate ester in ionic liquid
granting_institution	Universiti Putra Malaysia
publishDate	2012
url	http://psasir.upm.edu.my/id/eprint/67129/1/FS%202012%2096%20IR.pdf
_version_	1747812445484744704

Lipase-catalyzed preparation of galactose oleate ester in ionic liquid

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