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Comparison of gilthead sea bream ( Sparus aurata ) and hake ( Merluccius merluccius ) muscle proteins during iced and frozen storage
Author(s) -
Tejada Margarita,
Huidobro Almudena,
Mohamed Gamal Fouad
Publication year - 2002
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.1289
Subject(s) - hake , merluccius merluccius , merluccius , fishery , myosin , myosin atpase , biology , chemistry , fish <actinopterygii> , food science , atpase , biochemistry , enzyme
Gilthead sea bream ( Sparus aurata ) and hake ( Merluccius merluccius ) muscle behave differently during storage, whether in ice or deep frozen. Rapid changes have been observed in the texture of hake muscle during frozen storage, while gilthead sea bream has proved to be more stable. In order to ascertain the role of muscle proteins in the changes observed during storage, parameters related to protein functionality and the properties of extracted natural actomyosin (NAM) were studied initially and during storage in ice or at −20 °C. Initially, the parameters related to functionality had higher values in hake muscle and extracted NAM than in gilthead sea bream. At the end of iced storage (22 days), less myosin heavy chain (MHC) and actin were extracted from hake, but there was practically no change in gilthead sea bream. This decrease was not accompanied by lower Ca 2+ ‐ATPase activity. Freezing produced no drastic changes, with lower values for gilthead sea bream. However, this species was more stable after 1 year, except for the Ca 2+ ‐ATPase activity of NAM. This suggests that the changes that hake proteins underwent during storage particularly affected properties related to aggregation, whereas in gilthead sea bream the changes hardly affected the formation of soluble or insoluble aggregates but did affect the active sites of myosin. © 2002 Society of Chemical Industry