Bounded water kinetic model of beta-galactosidase in reverse micelles

In the present investigation, beta-galactosidase was solubilized into Aerosol OT (AOT)/isooctane reverse micelles. Kinetic data for the hydrolysis of o-nitrophenyl-beta-D-galactopyranoside (ONPG) at different pH values and molar ratios of water to AOT (Wo) were collected. It was observed that the us...

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Bibliographic Details
Published inBioprocess and biosystems engineering Vol. 26; no. 5; pp. 307 - 313
Main Authors Chen, C Will, Ou-Yang, Chao-Chih
Format Journal Article
LanguageEnglish
Published Germany 01.10.2004
Subjects
beta-Galactosidase - chemistry
Catalysis
Colloids - chemistry
Computer Simulation
Dioctyl Sulfosuccinic Acid - chemistry
Enzyme Activation
Kinetics
Micelles
Models, Chemical
Octanes - chemistry
Protein Binding
Water - chemistry
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Summary:In the present investigation, beta-galactosidase was solubilized into Aerosol OT (AOT)/isooctane reverse micelles. Kinetic data for the hydrolysis of o-nitrophenyl-beta-D-galactopyranoside (ONPG) at different pH values and molar ratios of water to AOT (Wo) were collected. It was observed that the usual kinetic model used for beta-galactosidase catalysis in aqueous systems failed to represent the experimental data. A bounded water model, however, showed a better correlation between enzymatic activity and Wo. In contrast to the aqueous system, controlling the water concentration in the reverse micelles allows the rate constants for the reaction between water molecules and glycosyl-enzyme complexes to be evaluated.
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ISSN:1615-7591
DOI:10.1007/s00449-004-0367-z