Effect of Ionic Strength and Temperature on Interaction between Fish Myoglobin and Myofibrillar Proteins

Authors

  • M. Chaijan,

    1. Authors Chaijan, and Benjakul are with the Dept. of Food Technology, Faculty of Agro-Industry, Prince of Songkla Univ., Hat Yai, 90112, Thailand. Author Visessanguan is with the Natl. Center for Genetic Engineering and Biotechnology, Natl. Science and Technology Development Agency, Pathumthani, 12120, Thailand. Authors Lee and Faustman are with the Dept. of Animal Science, Univ. of Connecticut, Storrs, CT 06269. Direct inquiries to author Faustman (E-mail: cameron.faustman@uconn.edu).
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  • S. Benjakul,

    1. Authors Chaijan, and Benjakul are with the Dept. of Food Technology, Faculty of Agro-Industry, Prince of Songkla Univ., Hat Yai, 90112, Thailand. Author Visessanguan is with the Natl. Center for Genetic Engineering and Biotechnology, Natl. Science and Technology Development Agency, Pathumthani, 12120, Thailand. Authors Lee and Faustman are with the Dept. of Animal Science, Univ. of Connecticut, Storrs, CT 06269. Direct inquiries to author Faustman (E-mail: cameron.faustman@uconn.edu).
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  • W. Visessanguan,

    1. Authors Chaijan, and Benjakul are with the Dept. of Food Technology, Faculty of Agro-Industry, Prince of Songkla Univ., Hat Yai, 90112, Thailand. Author Visessanguan is with the Natl. Center for Genetic Engineering and Biotechnology, Natl. Science and Technology Development Agency, Pathumthani, 12120, Thailand. Authors Lee and Faustman are with the Dept. of Animal Science, Univ. of Connecticut, Storrs, CT 06269. Direct inquiries to author Faustman (E-mail: cameron.faustman@uconn.edu).
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  • S. Lee,

    1. Authors Chaijan, and Benjakul are with the Dept. of Food Technology, Faculty of Agro-Industry, Prince of Songkla Univ., Hat Yai, 90112, Thailand. Author Visessanguan is with the Natl. Center for Genetic Engineering and Biotechnology, Natl. Science and Technology Development Agency, Pathumthani, 12120, Thailand. Authors Lee and Faustman are with the Dept. of Animal Science, Univ. of Connecticut, Storrs, CT 06269. Direct inquiries to author Faustman (E-mail: cameron.faustman@uconn.edu).
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  • C. Faustman

    1. Authors Chaijan, and Benjakul are with the Dept. of Food Technology, Faculty of Agro-Industry, Prince of Songkla Univ., Hat Yai, 90112, Thailand. Author Visessanguan is with the Natl. Center for Genetic Engineering and Biotechnology, Natl. Science and Technology Development Agency, Pathumthani, 12120, Thailand. Authors Lee and Faustman are with the Dept. of Animal Science, Univ. of Connecticut, Storrs, CT 06269. Direct inquiries to author Faustman (E-mail: cameron.faustman@uconn.edu).
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Abstract

ABSTRACT:  The effects of ionic strength (0, 0.3, and 0.6 M KCl) and temperature (4 and 25 °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 Ca2+-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 °C than at 4 °C (P < 0.05). Binding of myoglobin to NAM resulted in decreased whiteness (P < 0.05). Ca2+-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.

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