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The Properties of Covalently Immobilized Trypsin on Soap‐Free P(MMA‐EA‐AA) Latex Particles
Author(s) -
Kang Kai,
Kan Chengyou,
Yeung Anthony,
Liu Deshan
Publication year - 2005
Publication title -
macromolecular bioscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.924
H-Index - 105
eISSN - 1616-5195
pISSN - 1616-5187
DOI - 10.1002/mabi.200400178
Subject(s) - trypsin , chemistry , emulsion polymerization , carbodiimide , hydrolysis , polymer chemistry , immobilized enzyme , covalent bond , casein , chromatography , acrylate , methyl methacrylate , nuclear chemistry , polymerization , copolymer , organic chemistry , enzyme , polymer
Summary: The covalent immobilization of trypsin onto poly[(methyl methacrylate)‐ co ‐(ethyl acrylate)‐ co ‐(acrylic acid)] latex particles, produced by a soap‐free emulsion polymerization technique, was carried out using the carbodiimide method. The catalytic properties and kinetic parameters, as well as the stability of the immobilized enzyme were compared to those of the free enzyme. Results showed that the optimum temperature and pH for the immobilized trypsin in the hydrolysis of casein were 55 °C and 8.5, both of which were higher than that of the free form. It was found that K m (Michaelis constant) was 45.7 mg · ml −1 and V max (maximal reaction rate) was 793.0 μg · min −1 for immobilized trypsin, compared to a K m of 30.0 mg · ml −1 and a V max of 5 467.5 μg · min −1 for free trypsin. The immobilized trypsin exhibited much better thermal and chemical stabilities than its free counterpart and maintained over 63% of its initial activity after reusing ten times.TEM photograph of latex particles after trypsin immobilization.