Synthesis of Amphiphilic Polymer Particles by Seed Polymerization and Their Application for Lipase Immobilization

Autor:	Miho Kobayashi, Takuya Kotani, Atushi Ueda, Kouji Kawahara, Hibiki Nikaido, Haruo Ishikawa, Hiroyasu Ogino, Masahiro Yasuda
Rok vydání:	2002
Předmět:	Polymers and Plastics Immobilized enzyme biology Chemistry Organic Chemistry Dispersity Triacylglycerol lipase Porous glass Condensed Matter Physics Polymerization Amphiphile Polymer chemistry Materials Chemistry biology.protein Physical and Theoretical Chemistry Lipase Microparticle
Zdroj:	Macromolecular Chemistry and Physics. 203:284-293
ISSN:	1521-3935 1022-1352
DOI:	10.1002/1521-3935(20020101)203:2<284::aid-macp284>3.0.co;2-3
Popis:	To develop excellent immobilized enzymes, monodisperse amphiphilic polymer particles that have both hydrophilic guanidino groups and hydrophobic acyl groups were synthesized and characterized. The monodisperse amphiphilic particles, which had an average diameter of 7.92 μm, had macropores with diameters ranging from 50 nm to 500 nm. The amount of Rhizopus delemar lipase immobilized on the monodisperse amphiphilic polymer particles was 150-8 700 times those of the immobilized lipases prepared by previous investigators using Dowex MWA-1, porous glass beads, and Sepharose 4B. The specific transesterification activity of the immobilized lipase prepared with the monodisperse amphiphilic polymer particles was 93.4 times that of the lyophilized lipase.
Databáze:	OpenAIRE
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