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

TIRONI, V.A.; LOPEZ, L.B; PELLEGRINO, N; AÑÓN, M.C.; AND TOMÁS, M.C.

JOURNAL OF FOOD SCIENCE

Institute of Food Technologists

Año: 2004 vol. 69 p. 519 - 523

0022-1147

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 SDS, urea and b-mercaptethanol (ME), SDS-PAGE and available lysine determinations were performed in order to analyze the chemical nature of these alterations. Results showed notorious 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 non disulfide covalent bonds. A reduction in the available lysine content was evidenced due to the reaction of e-amino groups with MDA.