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Fatty acyl coupled catalase.

G Rosen1, J Bar-Tana

  • 1Department of Biochemistry, Hebrew University Medical School, Jerusalem, Israel.

Biochimica Et Biophysica Acta
|February 23, 1989
PubMed
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Bovine liver catalase was modified with fatty acids, altering its solubility and retaining significant enzymatic activity. This modification allows for further reactions with the enzyme

Area of Science:

  • Biochemistry
  • Enzyme Engineering
  • Protein Modification

Background:

  • Bovine liver catalase is a crucial enzyme for decomposing hydrogen peroxide.
  • Modifying enzyme properties can enhance their utility in various applications.
  • Fatty acylation is a method to alter protein solubility and membrane interactions.

Purpose of the Study:

  • To derivatize bovine liver catalase with a fatty acyl compound.
  • To investigate the impact of fatty acylation on catalase solubility and activity.
  • To explore potential downstream applications of the modified enzyme.

Main Methods:

  • Derivatization of bovine liver catalase using 9"(10")-[4'-(2-(4,6-dichloro-1,3,5-triazinyl) oxy)butoxy] stearic acid.
  • Separation of derivatized enzyme from native catalase and excess reagent via hydroxyapatite chromatography.

Related Experiment Videos

  • Assessment of enzyme solubility at different pH values and determination of residual enzymatic activities.

    • Main Results:

    • Fatty acyl residues were successfully coupled to lysine, histidine, and arginine residues of catalase.
    • The derivatized catalase exhibited pH-dependent solubility, being water-soluble at pH > 7.0 and octanol/ether-soluble at pH < 6.5.
    • The modified enzyme retained 50-80% of its original catalatic and peroxidative activities.
    • The carboxyl function of the fatty acyl chains remained available for CoA-thioesterification.

    Conclusions:

    • Fatty acylation effectively modifies bovine liver catalase, altering its solubility profile.
    • The derivatized catalase maintains significant catalytic functions, opening possibilities for new applications.
    • The modified enzyme's structure is amenable to further enzymatic modification, such as CoA-thioesterification.