Activity of Pseudomonas cepacia lipase in organic media is greatly enhanced after immobilization on a polypropylene support

The purified lipase from Pseudomonas cepacia was used as free and immobilized enzyme preparation for hydrolysis of p-nitrophenyl palmitate (pNPP) and p-nitrophenyl acetate (pNPA) in organic media. The free enzyme was mixed with bovine serum albumin and lyophilized. Immobilization was on porous polyp...

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Bibliographic Details
Published in:Applied microbiology and biotechnology 1997-06, Vol.47 (6), p.630-635
Main Authors: PENCREAC'H, G, BARATTI, J. C
Format: Article
Language:English
Subjects:
Biological and medical sciences
Biotechnology
Burkholderia cepacia
Burkholderia cepacia - enzymology
Diffusion
Enzymes
Enzymes, Immobilized - metabolism
Fundamental and applied biological sciences. Psychology
Heterogeneity
Identification and classification
Immobilization of enzymes and other molecules
Immobilization techniques
Immobilized enzymes
Kinetics
Lipase
Lipase - metabolism
Methods. Procedures. Technologies
Microbiological chemistry
Observations
Polypropylenes
Pseudomonas cepacia
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Description
Summary:The purified lipase from Pseudomonas cepacia was used as free and immobilized enzyme preparation for hydrolysis of p-nitrophenyl palmitate (pNPP) and p-nitrophenyl acetate (pNPA) in organic media. The free enzyme was mixed with bovine serum albumin and lyophilized. Immobilization was on porous polypropylene. Conditions where diffusional limitations of the substrate were not limiting the reaction rate were defined. The specific activity of the lipase was greatly enhanced upon immobilization: 16.5- and 7.8-fold for pNPP and pNPA respectively. Both the free and immobilized lipases followed Michaelis-Menten kinetics in organic solvent despite the heterogeneity (solid/liquid) of the reaction mixture. For pNPP, the activation factor upon immobilization came mainly from a reduction in Km)app while kcat was increased for pNPA.
ISSN:0175-7598
1432-0614
DOI:10.1007/s002530050986