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利用DSC对大豆蛋白质热变性的研究 被引量:63

Study on Soybean Protein Heating Denaturation by DSC
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摘要 利用差示扫描量热法 (DSC) ,对豆浆中的 2种主要大豆蛋白质β伴大豆球蛋白 (7S球蛋白 )和大豆豆球蛋白 (11S球蛋白 )的变性温度进行了试验研究。结果表明 :豆浆中 7S球蛋白的变性温度为 (70± 2 )℃ ,11S球蛋白的变性温度为 (90± 2 )℃ ;豆浆中固形物的质量分数 (5 .76~ 10 .37 )与 7S球蛋白和 11S球蛋白的变性温度呈显著的正相关关系。当加热到 70℃时 ,7S球蛋白变性 ;当加热到 95℃时 ,7S球蛋白和 The β conglycinin(7S) and glycinin(11S) exhibited respectively denaturation temperature of (70±2)℃ and (90±2)℃ in soymilk by DSC. Between solid contend of soymilk (5 76%~10 37%) and β conglycinin(7S) or glycinin(11S) denaturation temperature was positive. At 95 ℃, both 11S and 7S proteins were totally denatured, while at 70 ℃, the 7S protein was totally denatured but the 11S protein was not.
出处 《中国农业大学学报》 CAS CSCD 北大核心 2001年第6期93-96,共4页 Journal of China Agricultural University
基金 中日国际合作项目
关键词 DSC 大豆 蛋白质 热变性 球蛋白 β-conglycinin(7S) glycinin(11S) heat denaturation temperature
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参考文献5

  • 1[1]German B, Damodatan S, Kinsella J E. Thermal dissociation and association behavior of soy proteins. J Agric Food Chem, 1982,30(5):807~811
  • 2[2]Nakamura T, Utsumi S, Mori T. Effects of temperature on the different stages in thermal gelling of glycinin. J Agric Food Chem,1985,33(6):1201~1203
  • 3[3]Damodaran S. Refolding of thermally unfolded soy proteins during the colling regime of the gelation process: effect on gelation. J Agric Food Chem,1988,36(2):262~269
  • 4[4]Sorgentini D A, Wagner J R, Anon M C. Effects of thermal treatment of soy protein isolatate on the characteristics and structure-function relationship of soluble and insoluble fractions. J Agric Food Chem, 1995,43(9):2471~2479
  • 5[5]Wagner J R, Sorgentini D A, Anon M C. Thermal and electrophoretic behavior, hydrophobicity, and some functional properties of acid-theated soy isolatate. J Agric Food Chem,1996,44(7):1881~1889

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