Parallel enzymatic and non-enzymatic formation of zinc protoporphyrin IX in pork

TY - JOUR

T1 - Parallel enzymatic and non-enzymatic formation of zinc protoporphyrin IX in pork

AU - Miquel Becker, Eleonor-Carmen

AU - Westermann, Signe

AU - Hansson, Mats

AU - Skibsted, Leif Horsfelt

PY - 2012/2/15

Y1 - 2012/2/15

N2 - Zinc protoporphyrin is formed in pork homogenates in both enzymatic and non-enzymatic reactions. Ferrochelatase is active in formation of the highly fluorescent pigment known from Parma ham as demonstrated by inhibition with N-methylmesoporphyrin and by thermal inactivation. A non-enzymatic transmetallisation reaction, exchange of iron in myoglobin by zinc(II), is demonstrated by Pb(II) inhibition of zinc protoporphyrin formation at low Pb(II) concentrations, but promoted at higher Pb(II) concentrations. The non-enzymatic reaction is characterised as a slow bimolecular reaction between protoporphyrin IX and zinc(II) with a second-order rate constant of 0.63 l mol-1 s-1 at 35 °C and a high energy of activation of 98 kJ mol -1 for acetone:water (3:1, v/v) as solvent. Zinc protoporphyrin formation is concluded to be thermodynamically controlled with a formation constant of 4 × 105 M (35 °C, acetone:water (3:1)). An efficient inhibition of formation of zinc protoporphyrin by nitrite is related to myoglobin as substrate and involves both enzymatic and non-enzymatic reactions.

AB - Zinc protoporphyrin is formed in pork homogenates in both enzymatic and non-enzymatic reactions. Ferrochelatase is active in formation of the highly fluorescent pigment known from Parma ham as demonstrated by inhibition with N-methylmesoporphyrin and by thermal inactivation. A non-enzymatic transmetallisation reaction, exchange of iron in myoglobin by zinc(II), is demonstrated by Pb(II) inhibition of zinc protoporphyrin formation at low Pb(II) concentrations, but promoted at higher Pb(II) concentrations. The non-enzymatic reaction is characterised as a slow bimolecular reaction between protoporphyrin IX and zinc(II) with a second-order rate constant of 0.63 l mol-1 s-1 at 35 °C and a high energy of activation of 98 kJ mol -1 for acetone:water (3:1, v/v) as solvent. Zinc protoporphyrin formation is concluded to be thermodynamically controlled with a formation constant of 4 × 105 M (35 °C, acetone:water (3:1)). An efficient inhibition of formation of zinc protoporphyrin by nitrite is related to myoglobin as substrate and involves both enzymatic and non-enzymatic reactions.

U2 - 10.1016/j.foodchem.2011.07.090

DO - 10.1016/j.foodchem.2011.07.090

M3 - Journal article

SN - 0308-8146

VL - 130

SP - 832

EP - 840

JO - Food Chemistry

JF - Food Chemistry

IS - 4

ER -