Effect of ionic strength and temperature on interaction between fish myoglobin and myofibrillar proteins.
The effects of ionic strength (0, 0.3, and 0.6 M KCl) and temperature (4 and 25 degrees C) on the interaction between fish myoglobin and myofibrillar proteins were investigated in a model system. Increases in the relative content of bound myoglobin and metmyoglobin formation in myoglobin-natural actomyosin (NAM) mixtures with concurrent decreases in whiteness and Ca(2+)-ATPase activity were observed with increasing ionic strength (P < 0.05). The relative content of bound myoglobin and the oxidation of oxymyoglobin were generally greater at 25 degrees C than at 4 degrees C (P < 0.05). Binding of myoglobin to NAM resulted in decreased whiteness (P < 0.05). Ca(2+)-ATPase was not affected by temperature (P > 0.05). SDS-PAGE patterns of protein samples suggested that myoglobin-NAM interactions did not involve disulfide bonds. The formation of high-molecular-weight aggregates (>206 kDa) was observed and was more pronounced at higher ionic strength and higher temperature.
Chaijan
M
M
Dept. of Food Technology, Faculty of Agro-Industry, Prince of Songkla Univ., Hat Yai, 90112, Thailand.
Benjakul
S
S
Visessanguan
W
W
Lee
S
S
Faustman
C
C
D000205:Actomyosin / Q000737:chemistry; D000818:Animals; D004305:Dose-Response Relationship, Drug; D029941:Fish Proteins / Q000737:chemistry*; D005399:Fishes; D008970:Molecular Weight; D009124:Muscle Proteins / Q000737:chemistry; D009210:Myofibrils / Q000737:chemistry*; D009211:Myoglobin / Q000737:chemistry*; D009994:Osmolar Concentration; D013696:Temperature
D029941:Fish Proteins; D009124:Muscle Proteins; D009211:Myoglobin; D000205:Actomyosin