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Position: Home > Articles > Gelation Mechanism of Myosin Solution by T Goe FOOD SCIENCE 2002,23 (3) 49-54

谷氨酰胺转胺酶胶凝肌球蛋白的机理研究

作  者:
周红霞;江波
单  位:
无锡轻工大学食品学院;南京晓庄学院生命科学
关键词:
谷氨酰胺转胺酶;肌球蛋白;凝胶强度;凝胶
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。
译  名:
Gelation Mechanism of Myosin Solution by T Goe
作  者:
Zhou Hongxiaet al.
关键词:
Transglutaminase Myosin gel strength gel
摘  要:
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.

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