Kinetic studies and partial purification of peroxidase in wild pear
Journal Title: Scientific Journal of Pure and Applied Sciences - Year 2014, Vol 3, Issue 2
Abstract
Peroxidase,extracted from wild pears was isolated by ammonium sulfate precipitationtechnique and purified by ion exchange chromatography. The crude enzyme having19.5 U/mL activity and 1.3 U/mg specific activity was subjected to ammoniumsulfate precipitation technique for partial purification and the resultedactivity and specific activity were 16.5 U/mL and 3.17 U/mg respectively. Afterion exchange chromatography through DEAE-cellulose, fraction between 35-42exhibited maximum activity of 15 U/mL and specific activity of 7.14 U/mg. The enzyme under discussion was found to be quite activewith optimum temperature of 45oC. Optimum pH for the enzyme was 6.Thermal treatment of crude extract of wild pears peroxidase was more stable atpH 6. It was found that enzyme followed the Michealis-Menton mechanism and 21units/mg.protein and 70 mM were the calculated values for Vmax and Km inprecence of various concentrations of guaiacol and constant concentration ofH2O2. The results showed that wild pearperoxidase wasa thermostable enzyme. After 30 min at 60°C, the remaining activity was 35%.
Authors and Affiliations
S. Saeidian| Department of Biology, Payame Noor University, Iran
Keywords
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- EP ID EP320
- DOI 10.14196/sjpas.v3i2.1194
- Views 481
- Downloads 29
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