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大豆分离蛋白的双酶改性改善功能性的实验
Experiment of promote functional properties of soybean protein isolate by comprehensive modification
【摘要】 对大豆分离蛋白(SPI)进行传统改性,只可以改善一个或几个功能性,而SPI的溶解性和分子量不能兼得。利用中性蛋白酶和谷氨酰胺转胺酶(TG)对大豆分离蛋白进行复合改性,通过单因素和正交实验研究了中性蛋白酶酶解的最佳工艺条件:温度60℃、时间0.5h、pH7.0、酶用量4000U/g,SPI溶解性可达97.9%;再经过TG改性,所得的聚合物虽然有很大的分子量,还可以改善SPI的溶解性,并且乳化性、发泡性均有提高。
【Abstract】 Traditional modifying technology on soybean protein isolate (SPI), can improve only one or somefunctional properties of SPI, and we can′t have high solubility and high molecular weight simultaneously. Usingcomprehensive modification by neutral proteinase and transglutaminase on SPI, through odd factor tests and anorthogonalexperiment, the optimum conditions of enzymatic hydrolysis are temperature 60℃, operating time 0.5h,pH7.0, and enzyme concentration 4000U/g, the solubility of SPI can achieve 97.9%. Then modification by TG, cannot only have high molecular weight, but also can improve the solubility, emulsibility and foaming pro- perty ofSPI.
【Key words】 soybean protein isolate; neutral proteinase: transglutaminase; solubility;
- 【文献出处】 食品科技 ,Food Science and Technology , 编辑部邮箱 ,2005年12期
- 【分类号】TS201.25
- 【被引频次】19
- 【下载频次】313