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Freeze‐dried turkey muscle II.—Role of haem pigments as catalysts in the autoxidation of lipid constituents
Author(s) -
Fishwick M. J.
Publication year - 1970
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.2740210314
Subject(s) - metmyoglobin , autoxidation , myoglobin , chemistry , pigment , dehydration , catalysis , biochemistry , food science , chromatography , organic chemistry
A study by reflectance spectroscopy of the haem compounds of turkey breast and leg muscle showed that the structure of the main component, myoglobin, changed during the freeze‐drying process to form a low‐spin complex, ferromyochromagen. Ferrimyoglobin, either present in fresh muscle or introduced as an oxidation product during dehydration, forms the corresponding ferrimyochromagen. During storage in the freeze‐dried state the iron complexes do not catalyse the autoxidation of unsaturated lipids. When freeze‐dried muscle is rehydrated to a water content not less than 50% of that of fresh muscle, a proportion of the haem pigment is present in the form of a high‐spin complex, metmyoglobin, which catalyses autoxidation of unsaturated lipids in the rehydrated muscle.