title: Effect of ionic strength and temperature on interaction between fish myoglobin and myofibrillar proteins.
abstract: 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.
authors.affiliation: Dept. of Food Technology, Faculty of Agro-Industry, Prince of Songkla Univ., Hat Yai, 90112, Thailand.
authors.forename: M
authors.initials: M
authors.lastname: Chaijan
authors.forename: S
authors.initials: S
authors.lastname: Benjakul
authors.forename: W
authors.initials: W
authors.lastname: Visessanguan
authors.forename: S
authors.initials: S
authors.lastname: Lee
authors.forename: C
authors.initials: C
authors.lastname: Faustman
mesh_terms: 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
chemical_list: D029941:Fish Proteins; D009124:Muscle Proteins; D009211:Myoglobin; D000205:Actomyosin