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Interaction of Fish Myoglobin and Myofibrillar Proteins
Author(s) -
Chaijan M.,
Benjakul S.,
Visessanguan W.,
Lee S.,
Faustman C.
Publication year - 2008
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.1750-3841.2008.00749.x
Subject(s) - metmyoglobin , myoglobin , myofibril , myosin , chemistry , incubation , biochemistry , fish <actinopterygii> , atpase , biophysics , enzyme , biology , fishery
Interactions between fish myoglobin (Mb) and myofibrillar proteins were investigated in a Mb‐natural actomyosin (NAM) model at 4 °C. Increases in metmyoglobin (MetMb) formation and the relative content of bound Mb were observed, as were decreases in whiteness and Ca 2+ ‐ATPase activity ( P < 0.05). During the first 6 h of incubation, Mb bound preferably to myosin at domains other than the head portion, as evidenced by measurable ATPase activity. The potential binding of Mb to myosin heads occurred after 24‐h incubation as evidenced by the marked decrease in Ca 2+ ‐ATPase activity of the NAM–Mb mixture when compared to that of NAM alone ( P < 0.05). The interaction between fish Mb and myofibrillar proteins was more pronounced with increased storage time; formation of high‐molecular‐weight aggregates (> 206 kDa) also increased with time. Electrophoretic study revealed that disulfide bonds were not involved in Mb–NAM interactions.