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 | |
| Publication status | Published - Jul 2003 |
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All Science Journal Classification (ASJC) codes
- Chemistry(all)
- Chemical Engineering(all)
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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 journal › Article
}
TY - JOUR
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.
UR - http://www.scopus.com/inward/record.url?scp=0141730298&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0141730298&partnerID=8YFLogxK
U2 - 10.1252/kakoronbunshu.29.565
DO - 10.1252/kakoronbunshu.29.565
M3 - Article
AN - SCOPUS:0141730298
VL - 29
SP - 565
EP - 567
JO - Kagaku Kogaku Ronbunshu
JF - Kagaku Kogaku Ronbunshu
SN - 0386-216X
IS - 4
ER -