食品科学 ›› 2002, Vol. 23 ›› Issue (3): 49-54.

• 基础研究 • 上一篇    下一篇

谷氨酰胺转胺酶胶凝肌球蛋白的机理研究

 周红霞, 江波   

  1. 南京晓庄学院生命科学,无锡轻工大学食品学院
  • 出版日期:2002-03-15 发布日期:2012-02-13

Gelation Mechanism of Myosin Solution by T Goe

 ZHOU  Hong-Xia, JIANG  Bo   

  • Online:2002-03-15 Published:2012-02-13

摘要: 对10%的肌球蛋白体系而言,加入10u/g蛋白质的谷氨胺酰转胺酶获得最大凝胶强度的条件为温度35℃,PH=7.0,反应时间90min。高浓度的肌球蛋白溶液加入0.02%u/mg蛋白质的谷氨酰胺转胺酶,37℃保温60min,形成可倒置的凝胶。扫描电子显微镜(SEM)观察该凝胶,结果表明此凝胶形成了致密的三维网状结构。十二烷基硫酸钠-聚丙烯酰胺凝胶电泳(SDS-DAGE分析反应产物,发现随着反应时间的延长,单体蛋白的带在减少,相应形成的大分子聚合物的量在增加,这说明谷氨酰胺转胺酶通过催化蛋白质之间的共价交联,从而增强了蛋白质凝胶结构的强度。

关键词: 谷氨酰胺转胺酶, 肌球蛋白, 凝胶强度, 凝胶

Abstract: For 10%myosin concentration maximum gel strength was achieved when the solution was incubated with Trans glu taminase (T Gase loulg Protein)at 35℃,pH9.0 for 90min. Myosin solutions at higher concentrations turned to self-supporting gels at 37 ℃with addition of 0.02uT Gase/g Protein. The micno-stnuture of protein gels prepared by T Gase was visnalized by Scanning electron Microscopy (SEM)and if was found that gels had a turee-dimensional net work. Analysis of reaction products by SDS-Polyacry lamide gel electrophoresis (SDS-PAGE) indicted a decrease in intact protein monomers and the formation of ploymer uhich could not enter into the running gel with increasing reaction time. Results showed that T Gase treatmeat increased the strength of the protein network throagh ∈-(r-glutamyl) lysine crosslinks.

Key words: Transglutaminase , Myosin gel strength gel