Biochemical factors influencing metmyoglobin formation on beef from muscles of differing colour stability.

Autor:	O'Keeffe M; Meat Research Department, The Agricultural Institute, Dunsinea Research Centre, Castleknock, Co. Dublin, Ireland., Hood DE
Jazyk:	angličtina
Zdroj:	Meat science [Meat Sci] 1982 Nov; Vol. 7 (3), pp. 209-28.
DOI:	10.1016/0309-1740(82)90087-0
Abstrakt:	Biochemical parameters, such as oxygen consumption rate by muscle post mortem (OCR), depth of oxygen penetration into meat, rates of myoglobin oxygenation and deoxygenation and myoglobin content and succinic dehydrogenase activity, were determined for muscles of differing colour stability. Metmyoglobin reduction, in anoxia following oxidation with ferricyanide (MRA) and aerobically following oxidation with low pO(2) (ARA), were also determined. M. psoas major (poor colour stability) has higher enzymic activity than M. longissimus dorsi (good colour stability). This difference, together with the low myoglobin content in M. psoas major, results in relatively high OCR with consequent low oxygen penetration and rapid conversion of oxymyoglobin to myoglobin in M. psoas major, disposing it to rapid formation of metmyoglobin. Metmyoglobin reduction occurs both under anaerobic and aerobic conditions but no significant correlation is found between actual metmyoglobin reduction and rate of discoloration of different muscles. The most significant factor affecting colour stability of beef muscles appears to be their enzymic activity which determines the rate of myoglobin oxidation. (Copyright © 1982. Published by Elsevier Ltd.)
Databáze:	MEDLINE
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