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

Muneharu Goto, Chiaki Hatanaka, Kazuya Uezu, Masahiro Goto

Research output: Contribution to journalArticle

1 Citation (Scopus)

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 languageEnglish
Pages (from-to)565-567
Number of pages3
Journalkagaku kogaku ronbunshu
Volume29
Issue number4
DOIs
Publication statusPublished - Jul 2003

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Enzyme immobilization
Lipases
Esterification
Lipase
Polymer matrix
Immobilized Enzymes
Oleic acid
Oleic Acid
Hydrophobicity
Glycerol
Polymers
Enzymes
Polymerization
monoolein

All Science Journal Classification (ASJC) codes

  • Chemistry(all)
  • Chemical Engineering(all)

Cite this

Selective Esterification of Monoolein by Controlling the Hydrophbicity of Enzyme-Immobilization Matrixes. / Goto, Muneharu; Hatanaka, Chiaki; Uezu, Kazuya; Goto, Masahiro.

In: kagaku kogaku ronbunshu, Vol. 29, No. 4, 07.2003, p. 565-567.

Research output: Contribution to journalArticle

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