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Physicochemical properties of water-soluble myofibrillar proteins prepared from chicken breast muscle

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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.
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Keywords: freeze-dried protein powder; heating of myofibrillar proteins; re-solubilization in water; solubility of the proteins; water-soluble myofibrillar proteins

Document Type: Research Article

Affiliations: 1: R and D Center, Nippon Meat Packers Inc., Tsukuba-shi and 2: Graduate School of Agriculture, Kyushu University, Higashi-ku, Fukuoka-shi, Japan 3: Graduate School of Agriculture, Hokkaido University, Kita-ku, Sapporo-shi,

Publication date: February 1, 2004

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