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CHANGES IN MUSCLE PROPERTIES DURING POSTMORTEM STORAGE OF FARMED SEA BREAM ( SPARUS AURATA )
Author(s) -
SUÁREZ M.D.,
MARTÍNEZ T.F.,
SÁEZ M.I.,
ALFÉREZ B.,
GARCÍAGALLEGO M.
Publication year - 2011
Publication title -
journal of food process engineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.507
H-Index - 45
eISSN - 1745-4530
pISSN - 0145-8876
DOI - 10.1111/j.1745-4530.2009.00522.x
Subject(s) - myofibril , sarcoplasm , softening , flesh , electrophoresis , chemistry , food science , proteolysis , water holding capacity , fish <actinopterygii> , biochemistry , fishery , biology , enzyme , endoplasmic reticulum , statistics , mathematics
This study assesses the effects of storage temperature on postmortem changes in textural parameters (firmness, water holding capacity), and their relationship with biochemical and electrophoretic determinations (muscle collagen content and solubility, amount and integrity of sarcoplasmic and myofibrillar proteins) in sea bream muscle. Storage at 1C resulted in a prolongation of the firmness compared with 4C, with no noticeable changes in water holding capacity. This delay in muscle softening at 1C could be partially explained by a limited proteolysis of some myofibrillar proteins, although inconsistent tendency was observed for other fractions. In contrast, the rate of muscle collagen degradation was higher at 4C compared with 1C, this becoming the main contributing factor to firmness losses. The great variety of protein fractions separated electrophoretically, and the relatively minor and contradictory changes observed suggest the unfeasibility of electrophoresis as a routine procedure for studying freshness in stored sea bream.PRACTICAL APPLICATIONS According to the results obtained, it is strongly recommended that the storage of sea bream ( Sparus aurata ) throughout the commercial chain is carried out at 1C, instead of the usual temperature of 4C. This modification clearly delays the process of muscle softening, thus improving objective quality in this species. The electrophoretic separation of muscle proteins has been previously proposed as a suitable procedure for assessing the freshness of fish during cold storage. However, the results obtained here indicate that the attempts aimed to the development of an electrophoretic procedure for detecting modifications in muscle proteins that could be correlated with flesh textural properties were unsuccessful. This is especially true if short‐term deterioration is assessed.