한국환경보건학회지 (Journal of Environmental Health Sciences)

  • 제30권4호
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  • Pages.314-319
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  • 2004
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  • 1738-4087(pISSN)
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  • 2233-8616(eISSN)
한국환경보건학회 (Korean Society of Environmental Health)
권호 표지

Turbidity Profile of Maleylated Glycinin

  • Kim, Kang-Sung (Department of Food Science and Nutrition, Yongin University) ;
  • Kim, Myung-Hee (Department of Food Service & Culinary, Kyonggi University) ;
  • Kim Se-Ran (Division of Food Chemistry and Biotechnology, Korea Food Research Institute) ;
  • Kwon, Dae-Young (Division of Food Chemistry and Biotechnology, Korea Food Research Institute)
  • 발행 : 2004.11.01
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초록

Glycinin of more than $97\%$ purity was modified using maleic anhydride. Glycinin samples of $0\%,\;65\%,\;and\;95\%$ lysine residue modifications were used to determine the changes in turbidimetric characteristics of the protein due to maleylation. The solubility behavior of the protein as a function of pH was changed with maleylation. The isoelectric point of $65\%\;and\;95\%$ modified glycinin shifted to pH 4.0 and pH 3.5-4.0, respectively, as compared to pH 4.6 for native glycinin. Maleylated glycinins exhibited increased solubility at pH above 4.6. Turbidity of native glycinin decreased substantially by the addition of NaCl, but the stabilizing effect of NaCl decreased when the protein was chemically modified. The effect of NaCl on $65\%$ modified glycinin was intermediate between native glycinin and $95\%$ modified sample. Thermal aggregation of native glycinin was completed within 5 min of heating at $80^{\circ}C$. Maleylation contributed significantly to the thermostability of the protein at pH of 7.0 and 9.0, exhibiting little turbidity. Addition of NaCl suppressed thermal aggregation of native glycinin, but turbidity actually increased for the samples of $65\%\;and\;95\%$ modification.

키워드

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