Purification and Characterization of Peroxidase From Anthracnose Disease Infected Papaya (Carica papaya L.).
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Date
2013
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Abstract
Peroxidase enzyme was isolated and purified from the pulp of disease infected ripen papaya
of local variety by 90% ammonium sulphate precipitation, chromatography on DEAEcellulose
followed by hydrophobic chromatography on Phenyl Sepharose CL-4B and the
purifications achieved was about 7.2 fold with 2.5% recovery. The purified enzyme was
homogeneous as judged by polyacrylamide slab gel electrophoresis. The purified enzyme
had a Mr of about 55,000 and 50 000 as determined by gel filtration on Sephadex G-100
and SDS-PAGE, respectively. The molecular mass of the enzyme was found to be very
similar under both reducing and non-reducing conditions indicating that the enzyme
contains no subunit. The enzyme has the following characteristics: pH optima at 6.0,
temperature optima around 38°C, enzyme activity was found to be strongly inhibited in the
presence of potassium cyanide and Fe+2 while the activity was found to be remarkably
increased in the presence of ammonium sulphate. The Km value for the peroxidase obtained
with pyrogallol as substrate was 0.027 mM.
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Keywords
Papaya, Anthracnose disease, Peroxidase purification
Citation
Bari L, Hassan P, Absar N, Khatun S, Hossain MI. Purification and Characterization of Peroxidase From Anthracnose Disease Infected Papaya (Carica papaya L.). Bangladesh Journal of Medical Biochemistry. 2013; 6(2): 49-57.