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Physicochemical properties of water‐soluble myofibrillar proteins prepared from chicken breast muscle
Author(s) -
ITO Yukiko,
TOKI Shinji,
OMORI Takashi,
IDE Hiroshi,
TATSUMI Ryuichi,
WAKAMATSU Junichi,
NISHIMURA Takanori,
HATTORI Akihito
Publication year - 2004
Publication title -
animal science journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.606
H-Index - 38
eISSN - 1740-0929
pISSN - 1344-3941
DOI - 10.1111/j.1740-0929.2004.00156.x
Subject(s) - myofibril , solubility , chemistry , ionic strength , chromatography , solubilization , biochemistry , aqueous solution , organic chemistry
The solubility of skeletal muscle myofibrillar proteins in water was examined. The solubility of the proteins was found to be sensitive to ionic strength and pH of the solution. At the ionic strength of less than 12 mM and neutral pH, more than 80% of myofibrillar proteins were solubilized. Heating at a temperature of more than 70°C was required for the proteins to retain their solubility. The solubility of freeze‐dried protein powder prepared from water‐soluble myofibrillar proteins was also examined, and it was found that addition of trehalose and heating were essential for re‐solubilization in water. Amino acid composition of water‐soluble myofibrillar proteins was found to be almost the same as that of myofibrillar proteins.