Publicação: Soluble and bound peroxidases from papaya fruit
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Soluble and bound peroxidases were isolated from the pulp of ripening papaya fruit. During papaya ripening, soluble and bound peroxidase activities increased 2.5- and 4.2-fold, respectively. Soluble peroxidase was purified 59-fold by ammonium sulphate precipitation and chromatography on Sephadex G-25, DEAE-cellulose and Sephadex G-100. Bound peroxidase was purified 140-fold by ammonium sulphate precipitation and chromatography on Sephadex G-100 and DEAE-cellulose. Polyacrylamide gel electrophoresis of the purified preparations revealed that both enzymes were highly purified by the procedures adopted. The soluble and bound forms had a Mr of 41 000 and 54 000, respectively. Soluble and bound peroxidases showed optimum activity at pH 6.0 and 5.5, respectively, and were inhibited by p-chloromercuribenzoate, iodoacetamide, N-ethylmaleimide, potassium cyanide and Fe2+. Soluble peroxidase was activated by ammonium sulphate and this activation was prevented by cyanide. © 1990.
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Carica papaya, Caricaceae, enzyme properties., papaya fruit, peroxidase, ripening
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Inglês
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Phytochemistry, v. 29, n. 4, p. 1051-1056, 1990.
