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Kinetics of cholesterol oxidation by cholesterol oxidase

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Abstract

Kinetic studies of cholesterol oxidation catalyzed by soluble cholesterol oxidase fromBrevibacterium were conducted. The optimum temperature and pH were found to be 40–45°C and 7.0, respectively. A plot of initial reaction rate versus cholesterol concentration is sigmoidal in shape. Analysis of the data suggests that the reaction follows a concerted model and not a stepwise model.

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Abbreviations

[E o ]:

initial enzyme concentration

E R :

enzyme in strong binding (R) state

E T :

enzyme in weak binding (T) state

h :

Hill coefficient

K h :

association constant ofES h

K m :

Michaelis constant, mM

K m, app :

apparent Michaelis constant

K s1 ,K s2 :

dissociation constants in equation 2

K s1s2 :

dissociation or composite constant in equation 2

K R :

dissociation constant ofR state

K T :

dissociation constant ofT state

[S], [S1], [S2]:

substrate concentration

S h :

h number of substrate molecules bind to enzyme to form complexES h

R :

strong substrate binding state

T:

weak substrate binding state

v :

initial reaction rate, mM/min

V m :

maximum reaction rate, mM/min

Y :

fractional saturation of enzyme

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Authors and Affiliations

  1. Department of Chemical Engineering, Kingsbury Hall, University of New Hampshire, 03824, Durham, NH

    Palligarnai T. Vasudevan & Tao Zhou

Authors
  1. Palligarnai T. Vasudevan
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  2. Tao Zhou
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Vasudevan, P.T., Zhou, T. Kinetics of cholesterol oxidation by cholesterol oxidase. Appl Biochem Biotechnol 60, 63–72 (1996). https://doi.org/10.1007/BF02788060

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  • DOI: https://doi.org/10.1007/BF02788060

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