摘要
利用转谷氨酰胺酶(TG)催化大豆分离蛋白(SPI)进行交联,探讨不同温度、pH和盐离子条件下改性前后大豆分离蛋白的溶解性,并利用SDS-PAGE电泳技术对改性后的大豆分离蛋白组分进行了亚基分析,旨在为改性大豆分离蛋白在食品中的应用提供一定的参考。结果显示,与SPI相比,经TG酶改性后的大豆分离蛋白(MSPI)在不同处理条件下的溶解性均有明显下降;SDS-PAGE凝胶电泳结果显示,在不同温度下,14.4~22.0 ku的B-11S亚基不容易形成沉淀;在不同pH条件下,等电点附近沉淀的亚基数量最多而上清液中几乎没有,这与等电点附近溶解性的变化规律相符;在不同盐离子浓度下,MSPI溶液中的亚基种类未发生变化。
Transglutaminase(TG)was used to catalyze the crosslinking of soy protein isolate(SPI),and the solubility of SPI under different conditions of temperature,pH and salt ions was discussed.The subunit analysis of the modified SPI was carried out by SDS-PAGE electrophoresis.The results showed that the solubility of soybean protein isolate(MSPI)modified by TG enzyme decreased obviously under different treatment conditions compared with SPI.SDS-PAGE gel electrophoresis showed that the B-11S subunit between 14.4 ku and 22.0 ku was not easy to precipitate at different temperatures.Under different pH conditions,the number of precipitated subunits near the isoelectric point was the most,but there were almost no subunits in the supernatant,which was consistent with the change law of solubility near the isoelectric point.Under different salt ion concentrations,the subunit species in MSPI solution did not change.
作者
张志衡
王升楠
卢亚东
李玉娥
陈振家
ZHANG Zhiheng;WANG Shengnan;LU Yadong;LI Yu'e;CHEN Zhenjia(College of Food Science and Engineering,Shanxi Agricultural University,Taigu 030801,China)
出处
《山西农业科学》
2021年第3期376-381,共6页
Journal of Shanxi Agricultural Sciences
基金
山西省重点研发计划项目(201903D221035)
山西农业大学博士科研启动项目(2016ZZ06)。
