Linked Life Data

7764355

Source:http://linkedlifedata.com/resource/pubmed/id/7764355

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1994-3-2
pubmed:abstractText
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 CaCO3 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 CaCO3 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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
B
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
8756-7938
pubmed:author
pubmed:issnType
Print
pubmed:volume
9
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
661-5
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:articleTitle
Preparation of porous polyurethane particles and their use in enzyme immobilization.
pubmed:affiliation
Department of Chemical Engineering, State University of New York at Buffalo 14260-4200.
pubmed:publicationType
Journal Article