Artículos de revistas
Obtention Of A New Source Of Peroxidase From Copaifera Langsdorffii Leaf, Desf. With High Activity [obtenção De Nova Fonte De Peroxidase De Folha De Copaifera Langsdorffii Desf. Com Alta Atividade]
Registro en:
Ciencia E Tecnologia De Alimentos. , v. 26, n. 4, p. 735 - 739, 2006.
1012061
2-s2.0-34247622273
Autor
Maciel H.P.F.
Gouvea C.M.C.P.
Pastore G.M.
Institución
Resumen
The purpose of this work was to extract peroxidase from Copaifera langsdorffii leaves (COP), measure its activity, compare it to that of Horseradish peroxidase and determine the optimum pH, the best extraction solution and the effect of additives on the COP activity. The results showed that COP has 81.6% of the activity of HRP and an optimum pH range between 5.5-6.0. The best extraction solution was a sodium phosphate buffer 50 mM, pH 6.0 and the best additive was PVPP. In conclusion, COP presents higher activity than peroxidases from different sources reported in the literature. 26 4 735 739 ADAMS, J.B., Regeneration and the kinetics of peroxidase inactivation (1997) Food Chemistry, 60 (2), pp. 201-206 _ Review: Enzyme inactivation during heat processing of food-stuffs. 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