Scientific journal NRU ITMO
Series "Processes and Food Production Equipment"
Registration certificate ЭЛ № ФС 77 – 55245 от 04.09.2013
зарегистрировано в Федеральной службе по надзору в сфере связи, информационных технологий и массовых коммуникаций
ISSN:2310-1164

Декабрь 2014 (published: 03.12.2014)

Number 4(22)

Home > Issue > Stability of iron-porphyrin complexes red colo and properties of the ligand

UDC 644-4

Stability of iron-porphyrin complexes red colo and properties of the ligand

Paramonova A.P., Murashev S.V.

Storing red fresh meat is largely dependent on the stability of a bright red pigment of muscle tissue - oxymyoglobin. The problem is that oxymyoglobin able to spontaneous autoxidation. The set of processes initiated by oxidation of the iron ion of the heme group is accompanied by generation of reactive oxygen species and hydroxyl ions. Free radicals can destroy the porphyrin ring of heme and thus even more change red meat. The formation of hydroxyl ions, the pH shifts to the alkaline side, which creates the necessary conditions for the growth of microorganisms. Microorganisms in turn also change the red color of meat and accelerate its deterioration. Thus, the stability of red meat is closely linked to long-term preservation of its freshness. In this regard, requires identifying properties of a ligand capable of displacing oxygen in the heme myoglobin to form stable complexes with red iron-porphyrin.
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Keywords: myoglobin, heme, porphyrin ring, iron ion, ligands, polarizability.

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