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

Yukiko Ito; Shinji Toki; Takashi Omori; Hiroshi Ide; Ryuichi Tatsumi; Jun Ichi Wakamatsu; Takanori Nishimura; Akihito Hattori

doi:10.1111/j.1740-0929.2004.00156.x

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

Yukiko Ito, Shinji Toki, Takashi Omori, Hiroshi Ide, Ryuichi Tatsumi, Jun Ichi Wakamatsu, Takanori Nishimura, Akihito Hattori

Animal and Marine Bioresource Sciences

Research output: Contribution to journal › Article › peer-review

14 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	59-65
Number of pages	7
Journal	Animal Science Journal
Volume	75
Issue number	1
DOIs	https://doi.org/10.1111/j.1740-0929.2004.00156.x
Publication status	Published - Feb 2004

All Science Journal Classification (ASJC) codes

Medicine(all)

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10.1111/j.1740-0929.2004.00156.x

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title = "Physicochemical properties of water-soluble myofibrillar proteins prepared from chicken breast muscle",

abstract = "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.",

author = "Yukiko Ito and Shinji Toki and Takashi Omori and Hiroshi Ide and Ryuichi Tatsumi and Wakamatsu, {Jun Ichi} and Takanori Nishimura and Akihito Hattori",

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T1 - Physicochemical properties of water-soluble myofibrillar proteins prepared from chicken breast muscle

AU - Ito, Yukiko

AU - Toki, Shinji

AU - Omori, Takashi

AU - Ide, Hiroshi

AU - Tatsumi, Ryuichi

AU - Wakamatsu, Jun Ichi

AU - Nishimura, Takanori

AU - Hattori, Akihito

PY - 2004/2

Y1 - 2004/2

N2 - 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.

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

Abstract

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