摘要
以大豆低温脱脂豆粕为原料提取大豆分离蛋白(SPI),在传统碱溶酸沉法制备SPI的碱溶阶段采用不同程度的热处理(25、50、60、70、80℃),研究了碱溶热处理对SPI溶解度、热聚集和流变性质的影响。其结果表明,碱溶热处理破坏了SPI的溶解度,可溶性部分含有大量由二硫键结合的大分子聚集体。碱溶热处理能提高蛋白弹性模量的同时降低凝胶点温度。适当的碱溶热处理(60℃)不仅能保留较好的蛋白溶解度,还能获得最佳的凝胶弹性。
Soybean protein isolate(SPI) was prepared from low-heat defatted soy flour,and preheated during alkaline extraction. The effects of alkaline-heating treatment(25,50,60,70 and 80℃) on the solubility,thermal aggregation and rheological property of SPI were studied. The results showed that alkaline-heating treatment destroyed the protein solubility. The soluble portion of SPI samples contained a large number of aggregates which were mainly cross-linked by disulfide bonds. The alkaline-heating treatment could significantly improve the elastic modulus but decrease the gel point temperature of SPI samples. Alkaline-heating at 60℃ was proved to maintain a relatively fine solubility and exhibit the best elasticity of SPI.
出处
《食品工业科技》
CAS
CSCD
北大核心
2014年第16期101-104,共4页
Science and Technology of Food Industry
基金
国家863计划(2013AA102204)
中央高校基本科研业务费专项资金项目(JUSRP21108)
江南大学博士研究生科学研究基金项目
关键词
大豆分离蛋白
碱溶热处理
溶解度
热聚集
流变性质
soybean protein isolate
alkaline-heating
solubility
thermal aggregation
rheological property