作　　者： ; ;

机构地区： 华南理工大学轻工与食品学院食物蛋白工程研究中心

出　　处： 《中国粮油学报》 2010年第6期26-30,共5页

摘　　要： 系统比较了两种大豆蛋白分级方法所得蛋白组分的亚基组成、蛋白质得率以及组分流向、溶解性和乳化活性等物化性质和功能性质,结果表明两种方法的蛋白组分在不同性质上表现各有异同。Nagano的IM和Samoto的LP组分的亚基组成差异较大。Nagano组分总蛋白得率略高于Samoto。相对于7S组分,两种分级方法的大豆蛋白均更多地集中于11S和IM/LP组分。Nagano和Samoto法的蛋白质分别在11S和LP组分富集。11S和7S组分的脂量分布低于IM或LP组分,Samoto的LP组分脂分布率明显高于其他组分。Naga-no和Samoto蛋白组分等电点在pH4.5左右,Samoto的LP组分由于其较高脂含量而溶解度最低且对pH不敏感。Nagano和Samoto组分中7S组分的乳化活性较高,Samoto的LP由于其低溶解性而使乳化活性最低。 Characteristics of soy protein fractions generated with Nagano procedure or Samoto procedure in subunit composition,protein yield and ingredient distribution,solubility and emulsification were investigated.Results： The above characteristics differ between the fractionations from Nagano or Samoto procedure.Prominent difference in subunit composition is found between IM and LP fractions with reference to SDS-PAGE.Total protein yield of Nagano procedure is a little higher than Samoto procedure.More soy proteins are distributed in 11S and IM/LP fractions than in 7S fractions for both procedures.Soy proteins mostly are distributed in 11S fraction for Nagano procedure and in LP fraction for Samoto procedure.Fewer lipids are distributed in 11S and 7S fractions than in IM or LP fractions with LP richest in lipids than any other fraction.The isoelectronic points of protein fractions discussed above are pH 4.5.The solubility of LP produced from Samoto procedure is insensitive to pH in wide range.The emulsification activities are relatively high for both 7S-rich fractions with emulsification stabilities for both 11S-rich fractions.The emulsification activities of 11S-and 7S-rich fractions produced from Nagano procedure are superior to 11S-and 7S-rich fractions from Samoto procedure,whereas that of LP is inferior due to its undesirable solubility.

关 键 词： 大豆蛋白 分级 功能性质

领　　域： [农业科学]