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Cell-linked and extracellular cholesterol oxidase activities from Rhodococcus erythropolis. Isolation and

M Sojo1, R Bru, D Lopez-Molina

  • 1Departamento de Bioquímica y Biología Molecular (A), Facultad de Biología, Universidad de Murcia, Spain.

Applied Microbiology and Biotechnology
|May 1, 1997
PubMed
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Cholesterol induces Rhodococcus erythropolis to synthesize cholesterol oxidase (enzyme). This enzyme appears both cell-wall-bound and extracellular, requiring new protein synthesis and emulsified cholesterol for optimal induction.

Area of Science:

  • Microbiology
  • Enzymology
  • Biochemistry

Background:

  • Rhodococcus erythropolis exhibits low cholesterol oxidase activity in cholesterol-free media.
  • Cholesterol is a key substrate for microbial metabolism and enzyme induction.

Purpose of the Study:

  • To investigate the regulation of cholesterol oxidase synthesis and secretion in Rhodococcus erythropolis.
  • To characterize the relationship between cell-wall-bound and extracellular cholesterol oxidase forms.

Main Methods:

  • Culturing Rhodococcus erythropolis in media with and without cholesterol.
  • Inducing enzyme synthesis with emulsified cholesterol and Tween 80.
  • Assessing enzyme activity and protein synthesis using chloramphenicol.
  • Analyzing enzyme forms via electrophoresis and kinetic studies.

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Main Results:

  • Cholesterol addition significantly increased cholesterol oxidase synthesis, peaking at 6 days.
  • Extracellular enzyme appeared after intracellular enzyme accumulation.
  • De novo protein synthesis was essential for enzyme induction.
  • Enzyme levels decreased when cholesterol was removed.
  • Particulate and extracellular forms are likely different conformations of a 55 kDa enzyme.

Conclusions:

  • Cholesterol acts as an inducer for cholesterol oxidase production in Rhodococcus erythropolis.
  • The bacterium differentiates between cell-associated and secreted enzyme forms.
  • Enzyme regulation involves de novo protein synthesis and is dependent on substrate availability.