Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1978-1-27
pubmed:abstractText
Storage of frozen fish brings about a decrease of extractability of myofibrillar proteins. There is also deterioration of the texture and functional properties of the flesh. In model systems, aggregation of myosin, actin, tropomyosin, and whole myofibrils have been described. These changes are caused by concurrent action of partial dehydration due to the freezing out of water, exposure of the proteins to inorganic salts which are concentrated in the remaining nonfrozen fluid, interactions with free fatty acids liberated from phospholipids and with lipid oxidation products, and cross-linking by formaldehyde produced in some species of fish as a result of enzymic decomposition of trimethylamine oxide. The extent of protein alterations increases with time and temperature of storage as well as with advanced disintegration of the tissues and intermixing of their components. The role played by the individual factors and the significance of different types of bonds, i.e., hydrophobic adherences, ionic bonds, and covalent cross-links in particular cases are not yet fully disclosed. Retardation of the deteriorative changes of proteins in frozen fish is possible by avoiding high storage temperatures and oxidation of lipids, removing hematin compounds and other constituents promoting cross-linking reactions, and by adding cryoprotectors like sugars, several organic acids, amino acids, or peptides.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0099-0248
pubmed:author
pubmed:issnType
Print
pubmed:volume
8
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
97-129
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1976
pubmed:articleTitle
Protein changes in frozen fish.
pubmed:publicationType
Journal Article, Review