Porcine Plasma Proteins as a Surimi Protease Inhibitor: Effects on Actomyosin Gelation


  • W. Visessanguan,

    1. Author Visessanguan is with the National Center for Genetic Engineering and Biotechnology, National Science and Technology Development Agency, 73/1 Rama VI Rd. Rajdhevee, Bangkok 10400, Thailand.
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  • S. Benjakul,

    1. Author Benjakul is with the Department of Food Technology Faculty of Agro-Industry, Prince of Songkla University, Hat Yai, Songkhla, 90110, Thailand.
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  • H. An

    Corresponding author
    1. Author An is with the Department of Nutrition and Food Science, Auburn University, Alabama 36849.
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  • This work was in part supported by Grant No. E/2878-1 from the International Foundation for Science, Sweden, and Grant No. 98-35503-6384 from the U.S. Dept. of Agriculture-Cooperative State Research, Education, and Extension Service.

Direct correspondence to Dr. Haejung An (E-mail: anhaeju@ auburn.edu).


Effect of porcine plasma proteins (PPP) on thermal gelation of actomyosin in the presence and absence of fish proteinase was studied using a dynamic rheological test. Substantial decreases in development rate and magnitude of gel modulus were observed by the addition of proteinase to actomyosin gels. PPP was effective in protecting a myosin-heavy chain from proteolytic degradation, however, PPP itself interfered with the formation of actomyosin gel. Lower gel modulus was observed with actomyosin gels developed with higher concentrations of PPP added. Overall, PPP reversed the loss of gel modulus by the proteinase, however, the recovered gel modulus was only as high as those containing PPP only. These results implicated that, although PPP may revert autolytic activity in surimi, it interfaces with actomyosin gelation.