Antioxidative Ability of Chicken Myofibrillar Protein Developed by Glycosylation and Changes in the Solubility and Thermal Stability

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  • NISHIMURA Kimio
    Department of Food Science and Nutrition, Faculty of Human Life and Science, Doshisha Women’s College of Liberal Arts
  • MURAKOSHI Miki
    Department of Food Science and Nutrition, Faculty of Human Life and Science, Doshisha Women’s College of Liberal Arts
  • KATAYAMA Shigeru
    Department of Bioscience and Biotechnology, Faculty of Agriculture, Shinshu University
  • SAEKI Hiroki
    Graduate School of Fisheries Science, Hokkaido University

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Myofibrillar protein prepared from chicken breast muscle was incubated with several concentrations of glucose or maltose for 6 h at 60 °C and 35% relative humidity in order to obtain glycosylated chicken protein. When the ratio of the weights of the myofibrillar protein and glucose or maltose had respectively reached 1:6 or 1:3–5, the solubility of each type of glycosylated chicken protein in a 0.1 M NaCl solution was exceeded by about 60%, although the myofibrillar protein was insoluble in a low ionic strength solution. Moreover, when the myofibril and maltose reaction (myofibril:maltose = 1:4) was extended to 36 h, the glycosylated protein did not undergo denaturation when held at 50 °C for 2 h, while it also exhibited an antioxidative function against superoxide anion radicals.

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