TG催化鱼肉蛋白共价交联作用研究

Study on the Effect of Fish Protein Covalent Cross-linking Catalyzed by TG

以黑鲨鱼肌原纤维蛋白(MPI)、大豆分离蛋白(SPI)为原料,以谷氨酰胺转胺酶(TG)为蛋白质交联促进剂,采用SDS-PAGE电泳法和浊度法考察TG催化MPI和SPI共价交联的效果;从凝胶持水性、凝胶质构特性两方面探讨TG对MPI和SPI热诱导凝胶的影响.SDS-PAGE电泳图谱显示,在TG催化下,MPI和SPI的主要谱带颜色逐渐变淡,同时在图谱的上端出现的大分子蛋白带的颜色越来越深;浊度变化分析表明,在λ320nm处反应物的吸光值逐渐增大;TG催化和SPI的添加均能改善蛋白质的凝胶强度和持水性,且TG可以减少SPI对产品的不利影响.

Myofibrillar protein isolate （MPI） of the Black shark and soy protein isolate （SPI） were taken as raw materials, the transglutaminase as a protein cross-linking accelerator, and the SDS- polyacrylamide gel electrophoresis and the nephelometry were used to examine the effect of the covalent cross-linking between MPI and SPI by transglutaminase, the water-holding capacity and the texture were adopted to measure the influence of TG to the MPI and SPI gelatin. With the catalysis of TG, electrophoresis patterns of the proteins showed that the color of the major protein bands became lighter, while the color of the macromolecular protein band at the top of the map appeared deeper, and the nephelometry showed that the OD value （A320 nm）increased; the water-holding capacity and the gelatin strength were apparently improved by the catalysis of TG and the addition of SPI.