One-step purification and properties of catalase from leaves of Zantedeschia aethiopica

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Abstract

Catalase (E.C 1.11.1.6) was purified from leaves of Zandedeschia aethiopica to apparent homogeneity by a one-step hydrophobic interaction chromatography on a phenyl Sepharose CL-4B column. The purified enzyme preparation was obtained with a final recovery of enzyme activity of about 61% and a specific activity of 146 U/mg protein. The purified enzyme ran as a single protein band when analyzed both by native PAGE and SDS-PAGE corresponding to an Mrof 220,000 Da, which consists of 4 subunits with identical Mrof 54,000 Da. The pI of purified enzyme was found to be 5.2 by isoelectric focusing on ultrathin polycrylamide gels. The purified catalase has an optimum temperature of activity at 40°C, whereas it is stable between 0° and 50°C. As regards pH, the enzyme has an optimum activity of pH 7.0 and it is stable in the range pH 6-8. The absorption spectrum of the purified enzyme exhibited 2 peaks at 280 nm and 405 nm. © 1988.

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Trindade, H., Karmali, A., & Pais, M. S. (1988). One-step purification and properties of catalase from leaves of Zantedeschia aethiopica. Biochimie, 70(12), 1759–1764. https://doi.org/10.1016/0300-9084(88)90035-1

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