Selective Esterification of Monoolein by Controlling the Hydrophbicity of Enzyme-Immobilization Matrixes

Muneharu Goto; Chiaki Hatanaka; Kazuya Uezu; Masahiro Goto

doi:10.1252/kakoronbunshu.29.565

Selective Esterification of Monoolein by Controlling the Hydrophbicity of Enzyme-Immobilization Matrixes

Muneharu Goto, Chiaki Hatanaka, Kazuya Uezu, Masahiro Goto

Research output: Contribution to journal › Article › peer-review

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Abstract

Lipase from Rhizopus sp. was immobilized in the polymer matrix prepared by polymerization of n -vinyl-2-pyrrolidone, 2-hydroxymethacrylate or n-isopropylacrylamide. The esterification of oleic acid and glycerol was carried out at 310 K by using the immobilized lipase or free lipase. The selectivity of monoolein was dependent on the hydrohobicity of the polymer matrix immobilizing lipase. The hydrophilic polymer provided a high selectivity for monoolein in the esterification. It was found that controlling the hydrophobicity of the enzyme-immobilized matrix allowed the final constitution of the equilibrium state to be shifted.

Original language	English
Pages (from-to)	565-567
Number of pages	3
Journal	kagaku kogaku ronbunshu
Volume	29
Issue number	4
DOIs	https://doi.org/10.1252/kakoronbunshu.29.565
Publication status	Published - Jul 2003

All Science Journal Classification (ASJC) codes

Chemistry(all)
Chemical Engineering(all)

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title = "Selective Esterification of Monoolein by Controlling the Hydrophbicity of Enzyme-Immobilization Matrixes",

abstract = "Lipase from Rhizopus sp. was immobilized in the polymer matrix prepared by polymerization of n -vinyl-2-pyrrolidone, 2-hydroxymethacrylate or n-isopropylacrylamide. The esterification of oleic acid and glycerol was carried out at 310 K by using the immobilized lipase or free lipase. The selectivity of monoolein was dependent on the hydrohobicity of the polymer matrix immobilizing lipase. The hydrophilic polymer provided a high selectivity for monoolein in the esterification. It was found that controlling the hydrophobicity of the enzyme-immobilized matrix allowed the final constitution of the equilibrium state to be shifted.",

author = "Muneharu Goto and Chiaki Hatanaka and Kazuya Uezu and Masahiro Goto",

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journal = "Kagaku Kogaku Ronbunshu",

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T1 - Selective Esterification of Monoolein by Controlling the Hydrophbicity of Enzyme-Immobilization Matrixes

AU - Goto, Muneharu

AU - Hatanaka, Chiaki

AU - Uezu, Kazuya

AU - Goto, Masahiro

PY - 2003/7

Y1 - 2003/7

N2 - Lipase from Rhizopus sp. was immobilized in the polymer matrix prepared by polymerization of n -vinyl-2-pyrrolidone, 2-hydroxymethacrylate or n-isopropylacrylamide. The esterification of oleic acid and glycerol was carried out at 310 K by using the immobilized lipase or free lipase. The selectivity of monoolein was dependent on the hydrohobicity of the polymer matrix immobilizing lipase. The hydrophilic polymer provided a high selectivity for monoolein in the esterification. It was found that controlling the hydrophobicity of the enzyme-immobilized matrix allowed the final constitution of the equilibrium state to be shifted.

AB - Lipase from Rhizopus sp. was immobilized in the polymer matrix prepared by polymerization of n -vinyl-2-pyrrolidone, 2-hydroxymethacrylate or n-isopropylacrylamide. The esterification of oleic acid and glycerol was carried out at 310 K by using the immobilized lipase or free lipase. The selectivity of monoolein was dependent on the hydrohobicity of the polymer matrix immobilizing lipase. The hydrophilic polymer provided a high selectivity for monoolein in the esterification. It was found that controlling the hydrophobicity of the enzyme-immobilized matrix allowed the final constitution of the equilibrium state to be shifted.

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Selective Esterification of Monoolein by Controlling the Hydrophbicity of Enzyme-Immobilization Matrixes

Abstract

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