Food Research Institute, Toyama Prefectural Agricultural, Forestry and Fisheries Research Center, Yoshioka 360, Toyama 939-8153, Japan.
Food Chem. 2013 Sep 1;140(1-2):39-43. doi: 10.1016/j.foodchem.2013.01.103. Epub 2013 Feb 10.
The mechanism underlying the freeze-thaw fractionation of 7S and 11S globulins in soymilk was investigated. Freeze-thawed soymilk demonstrated an increased particle size compared with raw soymilk. Further, when defatted raw soymilk was freeze-thawed, it was fractionated into 7S (supernatant) and 11S (precipitate) globulins, similar to what is found with freeze-thaw of raw soymilk. When raw soymilk samples with different ratios of 11S/7S were freeze-thawed, the 11S-deficient variety showed no precipitate. The addition of sodium sulphite or sodium dodecyl sulphate also inhibited precipitate formation after freeze-thawing, resulting in no fractionation. These results suggest that the fractionation is due to selective precipitation of aggregates of 11S globulins and/or 11S globulins and lipid complexes, in which the protein molecules interact through disulphide bonds and/or hydrophobic interactions.
研究了豆浆中 7S 和 11S 球蛋白的冻融分级的机理。与生豆浆相比，冻融豆浆的粒径增大。此外，当脱脂生豆浆被冻融时，它会被分成 7S（上清液）和 11S（沉淀物）球蛋白，这与生豆浆的冻融情况相似。当用不同 11S/7S 比例的生豆浆进行冻融时，缺乏 11S 的品种没有沉淀物。添加亚硫酸钠或十二烷基硫酸钠也抑制了冻融后的沉淀形成，从而没有分级。这些结果表明，分级是由于 11S 球蛋白和/或 11S 球蛋白和脂质复合物的聚集体的选择性沉淀所致，其中蛋白质分子通过二硫键和/或疏水相互作用相互作用。
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