Enzyme immobilization on amphiphilic polymer particles having grafted polyionic polymer chains
作者： Masahiro Yasuda , Hibiki Nikaido , Wilhelm R. Glomm , Hiroyasu Ogino , Kosaku Ishimi
DOI: 10.1016/J.BEJ.2009.06.011
关键词: Chemistry 、 Polymer 、 Allylamine 、 Dispersity 、 Lipase 、 Polymerization 、 Immobilized enzyme 、 Amphiphile 、 Transesterification 、 Polymer chemistry
摘要: Abstract Previously, we have shown that amphiphilic polymer particles functionalized with both hydrophilic guanidino groups and hydrophobic acyl been to immobilize a large amount of lipase the immobilized retaining high transesterification activity in organic solvent. However, stability solvent was found be insufficient. In present study, chemical environment surrounding enzyme made more order enhance For this purpose, polyionic chains containing amino group addition were introduced. Monodisperse acrylic (∼10 μm) synthesized by seed polymerization presence pore forming agent, subsequently modified poly(allylamine) various reagents introduce functional groups. The half-life Rhizopus delemar on these macroporous hexane 2.46 times compared stearoyl
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