Interaction of fish myoglobin and myofibrillar proteins.
Interactions between fish myoglobin (Mb) and myofibrillar proteins were investigated in a Mb-natural actomyosin (NAM) model at 4 degrees 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.
Chaijan
M
M
Department of Food Technology, School of Agricultural Technology, Walailak University, Nakhon Si Thammarat, 80160, Thailand.
Benjakul
S
S
Visessanguan
W
W
Lee
S
S
Faustman
C
C
D000205:Actomyosin / Q000737:chemistry / Q000378:metabolism; D000818:Animals; D000252:Calcium-Transporting ATPases / Q000378:metabolism*; D029941:Fish Proteins / Q000737:chemistry / Q000378:metabolism*; D008970:Molecular Weight; D009124:Muscle Proteins / Q000737:chemistry / Q000378:metabolism*; D009210:Myofibrils / Q000737:chemistry / Q000378:metabolism*; D009211:Myoglobin / Q000737:chemistry / Q000378:metabolism*; D013696:Temperature; D013997:Time Factors; D014413:Tuna
D029941:Fish Proteins; D009124:Muscle Proteins; D009211:Myoglobin; D000205:Actomyosin; D000252:Calcium-Transporting ATPases