Malonaldehyde-induced microstructural modifications in myofibrillar proteins of sea salmon (Pseudopercis semifasciata)

Myofibrillar proteins of sea salmon were incubated with malonaldehyde (MDA) at 27 degrees C from 0 to 8 h. Microstructural modifications were investigated by transmission electron microscopy. Protein solubility in the presence of sodium dodecyl sulfate (SDS), urea and beta-mercaptethanol (ME), SDS-p...

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Bibliographic Details
Published in:Journal of food science 2004-09, Vol.69 (7), p.519-523
Main Authors: Tironi, V.A, Lopez, L.B, Pellegrino, N, Anon, M.C, Tomas, M.C
Format: Article
Language:English
Subjects:
animal proteins
available lysine
Biological and medical sciences
chemical bonding
chemical reactions
Fish
Fish and seafood industries
Food industries
Food science
Fundamental and applied biological sciences. Psychology
lysine
malonaldehyde
malondialdehyde
marine fish
microstructure
myofibrillar proteins
myofibrils
myosin
protein aggregates
protein binding
protein microstructure
protein structure
Proteins
Pseudopercis semifasciata
solubility
solvents
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Summary:Myofibrillar proteins of sea salmon were incubated with malonaldehyde (MDA) at 27 degrees C from 0 to 8 h. Microstructural modifications were investigated by transmission electron microscopy. Protein solubility in the presence of sodium dodecyl sulfate (SDS), urea and beta-mercaptethanol (ME), SDS-polyacrylamide gel electrophoresis (PAGE), and available lysine determinations were performed to analyze the chemical nature of these alterations. Results showed noteworthy microstructural changes and protein aggregation, involving myosin and other myofibrillar proteins. A large proportion of these aggregates was insoluble when treated with SDS, urea, and ME, suggesting the presence of nondisulfide covalent bonds. A reduction in the available lysine content was evidenced because of the reaction of epsilon-amino groups with MDA.
ISSN:0022-1147
1750-3841
DOI:10.1111/j.1365-2621.2004.tb13645.x