Premium
Tissue degradation, amino acid liberation and bacterial decomposition of bulk stored capelin
Author(s) -
Aksnes Anders,
Brekken Bjørn
Publication year - 1988
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.2740450107
Subject(s) - histidine , cadaverine , amino acid , putrescine , lysine , arginine , biochemistry , chemistry , tyrosine , glycine , serine , capelin , aspartic acid , histidine decarboxylase , food science , biology , enzyme , fish <actinopterygii> , fishery
Bulk stored capelin with high contents of feed in the gut is easily solubilised because of high proteolytic activity. The amino acids most quickly liberated are arginine, serine, histidine, leucine, lysine and tyrosine; glycine, aspartic acid and glutamic acid are liberated at a slower rate. Bacterial activity results in a rapid and considerable decrease in total amounts of tyrosine, lysine, serine, arginine and histidine. The main products formed by bacterial decomposition of lysine, histidine and arginine are cadaverine, histamine and putrescine, respectively. Storage of capelin in the presence of antibiotics increased the amounts of free amino acids and total amino acids. After 10 days' storage at 6°C, about 30% of the total amino acid content in fish treated with antibiotics were fee amino acids.