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Malonaldehyde‐induced Microstructural Modifications in Myofibrillar Proteins of Sea Salmon ( Pseudopercis semifasciata )
Author(s) -
Tironi V.A.,
Lopez L.B.,
Pellegrino N.,
Añtón M.C.,
Tomás M.C.
Publication year - 2004
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.2004.tb13645.x
Subject(s) - myofibril , chemistry , myosin , covalent bond , lysine , sodium dodecyl sulfate , urea , solubility , biochemistry , polyacrylamide gel electrophoresis , gel electrophoresis , sodium , protein aggregation , chromatography , amino acid , organic chemistry , enzyme
Myofibrillar proteins of sea salmon were incubated with malonaldehyde (MDA) at 27 °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 β‐mercaptethanol (ME), SDS‐polyacrylamide gel electrophore‐sis (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 e‐amino groups with MDA.