Proteolysis involvement in zinc-protoporphyrin IX formation during Parma ham maturation

Author(s)

Grossi, Alberto B. ^[1] ; do Nascimento, Eduardo S. P. ^[2] ; Cardoso, Daniel R. ^[2] ; Skibsted, Leif H. ^[1]

Affiliation

^[1] Univ Copenhagen, Dept Food Sci, DK-1958 Frederiksberg C - Denmark

^[2] Univ Sao Paulo, Inst Quim Sao Carlos, BR-13560970 Sao Carlos, SP - Brazil

• Document type: Journal article
• Source: Food Research International; v. 56, p. 252-259, FEB 2014.
• Web of Science Citations: 20

Abstract

During maturation of Parma ham a continuing increase in concentration of glycerol, choline, and free amino acids, as followed for 15 months by high resolution H-1 NMR of ham extracts, indicates activity of lipolytic and proteolytic enzymes. Proteolysis was shown to be mediated by endogenous cathepsins with detectable activity even at the latest stage of maturation. The concentration of red proteinous pigments containing zinc-protoporphyrin-IX (Zn-PP), as measured by fluorescence spectroscopy, increased throughout the whole maturation period concomitant with formation of low molecular weight peptides. EPR spectroscopy showed that the concentration of the high-spin iron(III) species metmyoglobin present at early stages of production, decreased during maturation to form a EPR-silent pigment suggested to be labile, partly proteolyzed iron(II) myoglobin gradually loosing iron forming non-heme colloidal ferric hydroxide. Proteolytic degradation of myoglobin and precipitation of inorganic iron(III) in the meat matrix are essential for the metal exchange to form Zn-PP and non-heme iron(III) species. (C) 2014 Elsevier Ltd. All rights reserved. (AU)

• FAPESP's process: 11/51555-7 - Bread and meat for the future
• Grantee: Daniel Rodrigues Cardoso
• Support type: Regular Research Grants
• FAPESP's process: 12/20507-0 - New methods in Meat Analyses: LC-DAD-SPE and MAD-DOSY
• Grantee: Eduardo Sanches Pereira Do Nascimento
• Support type: Scholarships in Brazil - Post-Doctorate