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Synthesis of Amphiphilic Polymer Particles for Lipase Immobilization
Author(s) -
Yasuda Masahiro,
Kasahara Hiroki,
Kawahara Kouji,
Ogino Hiroyasu,
Ishikawa Haruo
Publication year - 2001
Publication title -
macromolecular chemistry and physics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.57
H-Index - 112
eISSN - 1521-3935
pISSN - 1022-1352
DOI - 10.1002/1521-3935(20011101)202:16<3189::aid-macp3189>3.0.co;2-e
Subject(s) - amphiphile , lipase , chemistry , polymer , polymer chemistry , organic chemistry , immobilized enzyme , transesterification , enzyme , copolymer , catalysis
To develop a novel support of enzymes for use in the enzymatic reactions in organic media, amphiphilic polymer particles which have both a hydrophilic amino group and hydrophobic acyl group were synthesized. Using Rhizopus delemar lipase as a model enzyme, the effects of the kinds of the amino group and the number of carbon atoms in the chain of the acyl group of the amphiphilic polymer particles on the amount of lipase immobilized, and the organic solvent stability and the transesterification activity of the immobilized lipase in hexane were studied. Amphiphilic polymer particles in which a guanidino group and stearoyl group were introduced as the amino group and the acyl group, respectively, were the best particles that we tested in the present work.