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Structural and Functional Changes in Myofibrillar Proteins of Sea Salmon ( Pseudopercis semifasciata ) by Interaction with Malonaldehyde (RI)
Author(s) -
Tironi V.A.,
Tomás M.C.,
Añón M.C.
Publication year - 2002
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.1365-2621.2002.tb09430.x
Subject(s) - myofibril , myosin , chemistry , denaturation (fissile materials) , cooperativity , covalent bond , solubility , biophysics , thermal stability , biochemistry , biology , organic chemistry , nuclear chemistry
Changes on the myofibrillar proteins of Sea Salmon ( Pseudopercis semifasciata ) induced by malonaldehyde were investigated. Electrophoretic patterns, solubility, and differential scanning calorimetric studies were performed after incubation of proteins with malonaldehyde (MDA) at 27 °C. Results obtained showed a different thermal behavior, evidencing a decrease in thermal stability, changes in denaturation enthalpies values (ΔH total and ΔH myosln ), and the appearance of new molecular species with a loss in the cooperativity of the myosin denaturation. A decrease in solubility and SDS‐PAGE profiles revealed the participation of myosin and other proteins in the formation of aggregates involving nondisulfide covalent linkages for myosin heavy chain (MHC) and disulfide bridges in some other proteins.