Growth of Pseudomonas chlororaphis on apolyester–polyurethane and the purification andcharacterization of a polyurethanase–esterase enzyme
1999; Elsevier BV; Volume: 43; Issue: 1-2 Linguagem: Inglês
10.1016/s0964-8305(98)00057-2
ISSN1879-0208
AutoresGary T. Howard, Carmen Ruiz, Newton P. Hilliard,
Tópico(s)Microbial bioremediation and biosurfactants
ResumoA Pseudomonas chlororaphis was found to degrade and utilize apolyester polyurethane as a sole carbon and energy source. Polyurethane utilization by P.chlororaphis followed simple Michaelis–Menten kinetics. The Ks and μmax values were 0.802 mg·ml−1 and 1.316 doublings·h−1, respectively. The enzymes from P. chlororaphis responsible for polyurethanedegradation were found to be extracellular. Analysis of the polyurethane degrading proteins, usingnon-denaturing polyacrylamide gel electrophoresis, revealed three active protein bands with Rf values of 0.25, 0.417 and 0.917. A polyurethane degrading enzyme was purifiedand displayed esterase activity. This enzyme was inhibited by phenylmethylsulfonyl fluoride andhad a molecular weight of 27,000 daltons.
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