Premium
Covalent binding of a nerve agent hydrolyzing enzyme within polyurethane foams
Author(s) -
LeJeune Keith E.,
Russell Alan J.
Publication year - 2000
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/(sici)1097-0290(19960820)51:4<450::aid-bit8>3.0.co;2-h
Subject(s) - paraoxon , polyurethane , hydrolysis , immobilized enzyme , covalent bond , chemistry , adsorption , substrate (aquarium) , aqueous solution , polymer , polymerization , chromatography , chemical engineering , polymer chemistry , enzyme , organic chemistry , oceanography , engineering , acetylcholinesterase , geology
A phosphotriesterase preparation, extracted from Escherichia coli DH5α cells, was immobilized within a polyurethane foam matrix during polymer synthesis. The enzyme‐foam interaction was shown to be covalent and analysis of the hydrolysis of paraoxon in aqueous solution demonstrated that more than 50% of the initial enzyme specific activity was retained after immobilization in the foam. Factors affecting the rate of paraoxon degradation include foam hydrophobicity, the degree of mixing applied to initiate polymerization, and foam pretreatment prior to use in substrate hydrolysis. The storage stability of the foam is significant, with phosphotriesterase‐foam activity profiles exhibiting a three month half‐life. Foams are currently being developed for biocatalytic air filtering, in which gaseous substrates will be simultaneously adsorbed and degraded by the immobilized enzyme system. © 1996 John Wiley & Sons, Inc.