Isolation, purification, and characterization of catalase from the methylotrophic yeast Pichia pastoris.

Catalase (CATpp) with molecular weight 223 kD was isolated from the methylotrophic yeast Pichia pastoris and purified 90-fold by ion-exchange chromatography and gel filtration. Quantitative parameters of absorption and CD spectra of CATpp solutions and of its membrane-concentrated form (CATpp-conc) were studied. Rates of H2O2 decomposition and kinetic characteristics Km and kcat of CATpp and CATpp-conc were determined in 10 mM phosphate buffer (pH 7.

Comparative kinetic characterization of catalases from Candida boidinii yeast and bovine liver.

Catalase with molecular weight 230 +/- kD was isolated and purified from methylotrophic yeasts Candida boidinii by ion-exchange chromatography. The kinetic characteristics of yeast and bovine liver catalases were compared in the reaction of H2O2 decomposition using a wide range of H2O2 concentrations (up to 0.12 M) and PH (2-10).