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Characterization of cholesterol oxidase activity in AOT-isooctane reverse micelles and its dependence on micelle size

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Summary

Characterization of cholesterol oxidase in AOT reverse micelles was performed. pH and temperature profiles show that the entrapment of the enzyme does not change its characteristics appreciably. The enzyme tends to behave as it does in water when micelle size increases and does not maximum rate at some intermediate micelle size. Km was 55–60 fold that in water

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Abbreviations

AOT:

Dioctyl sodium sulfosuccinate

CTAB:

Cetyl trimethylamonium bromide

K1E :

Equilibrium constant of the enzyme between free and bound water

K2E :

Equilibrium constant of the enzyme between bound water and surfactant

kf:

Catalytic constant in free water

kb:

Catalytic constant in bound water

ks:

Catalytic constant in surfactant

n:

Number of water molecules strongly bound to one surfactant molecule

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Authors and Affiliations

  1. Departamento de Bioquimica. Facultad de Biología, Universidad de Murcia, E30001, MURCIA, Spain

    Roque Bru, Alvaro Sánchez-Ferrer & Francisco García-Carmona

Authors
  1. Roque Bru
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  2. Alvaro Sánchez-Ferrer
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  3. Francisco García-Carmona
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Bru, R., Sánchez-Ferrer, A. & García-Carmona, F. Characterization of cholesterol oxidase activity in AOT-isooctane reverse micelles and its dependence on micelle size. Biotechnol Lett 11, 237–242 (1989). https://doi.org/10.1007/BF01031570

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