摘要
目的:利用中性蛋白酶和谷氨酰胺转胺酶(TG)对大豆分离蛋白(SPI)进行复合改性,探讨对其功能性的影响。方法:通过单因素和正交实验以及电泳分析,研究了中性蛋白酶和TG对SPI的影响趋势。结果:中性蛋白酶作用的最佳工艺条件为温度60℃、时间0.5h、pH7.0、酶用量4000U/g,SPI溶解性可达97.9%。结论:经中性蛋白酶作用后,再经过TG改性,所得的聚合物不仅有很大的相对分子质量,还可以改善SPI的溶解性,并且乳化性、发泡性均有提高。
Objective： Using comprehensive modification by neutral proteinase and transglutaminase on SPI, functional properties of soybean protein isolate（SPI） were studied. Methods： Through odd factor and orthogonal experiment and electrophoresis analysis, the influence trends of neutral proteinase and transglutaminase were studied. Result： The optimum conditions of enzymatic hydrolysis are 60℃, operating time 0.5 h, pH7.0, enzyme concentration 4000 U/g, and the solubility of SPI is up to 97.9%. Conclusion： The comprehensive modification by neutral proteinase and transglutaminase can not only obtain high molecular weight, hut also improve the solubility, emulsibility and foaming property of SPI.
出处
《生物技术通讯》
CAS
2006年第1期49-51,共3页
Letters in Biotechnology
基金
辽宁省科技厅科技公关项目(2004205001)
关键词
大豆分离蛋白
中性蛋白酶
谷氨酰胺转胺酶
功能性
soybean protein isolate
neutral proteinase： transglutaminase
functional properties
