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Preparation of Porous Polyurethane Particles and Their Use in Enzyme Immobilization
Author(s) -
Wang X.,
Ruckenstein E.
Publication year - 1993
Publication title -
biotechnology progress
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 129
eISSN - 1520-6033
pISSN - 8756-7938
DOI - 10.1021/bp00024a015
Subject(s) - polyurethane , chemical engineering , adsorption , lipase , polymer , glutaraldehyde , isocyanate , adipic acid , immobilized enzyme , scanning electron microscope , chemistry , materials science , porosity , hydrolysis , polymer chemistry , organic chemistry , composite material , enzyme , engineering
Porous polyurethane particles were prepared as follows: (1) Two low molecular weight polymers, namely, poly[methylene(polyphenyl isocyanate)] and poly(propylene glycol) were mixed with stirring at room temperature and allowed to react. (2) The reacted mixture was dispersed with stirring in mineral oil containing small amounts of water, the catalyst dibutyltin dilaurate, and CaCO 3 powder. In the presence of the catalyst, the reaction between the two polymers proceeded to completion. Small particles of polyurethane are thus formed which contain mineral oil and CaCO 3 as porogens. The particles obtained, separated by filtration, were treated with a solution of HCl in order to generate additional pores, extracted with benzene to eliminate the mineral oil present in the pores, and finally subjected to drying and sieving. The particles were investigated by scanning electron microscopy (SEM), infrared (IR) spectroscopy, and specific surface area measurements. Lipase from Candida rugosa was immobilized by adsorption on the porous polyurethane particles and cross‐linked with glutaraldehyde to enhance the stability of the immobilization. The biocatalytic particles were used for the hydrolysis of triacylglycerides. The high activity of the immobilized enzyme, which per enzyme molecule can be higher than that of the free enzyme, reveals that the porous polyurethane particles constitute excellent supports for lipase.