摘要
通过十二烷基磺酸钠聚丙烯酰胺凝胶电泳(SDS-PAGE)研究不同热处理温度条件下转谷氨酰胺酶(TG)催化大豆分离蛋白(SPI)和肌原纤维蛋白(MPI)的凝胶特性.在超纯水环境中用TG处理SPI,在大于50 ℃的加热条件下所有SPI组分(除了球蛋白B亚基)都共价结合成大的杂聚物而无法进入分离胶.TG处理MPI后,所有MPI成分[除肌动蛋白(Actin)外],在60～90 ℃均能交联,并形成有序的高弹性凝胶结构.经TG处理的MPI/SPI混合蛋白,大量SPI使肌球蛋白重链和肌动蛋白变为低分子多肽,同时,TG催化MPI与SPI交联在进样端产生1条深色电泳条带(大豆蛋白中除基本亚基外的7S和11S两个亚基).
It was studied by SDS-PAGE technique that the gelation reaction of myofibrillar（MPI） and soy protein isolate （SPI） mixture catalysed by transgluminase （TG） at different temperatures. A substantial amount of cross-linking of SPI with TG treatments in deionized water occurred at above 50℃. Essentially all the SPI constituents, except the basic subunits （B） of glyeinin, were linked covalently forming a streak of polymers most of which were too large to enter the separating gel. All the MPI components, except actin, were cross-linked by TG at about 60 -90℃ ,but the products （gel） were most likely of an ordered structure because they exhibited a high elasticity. For heated MPI/SPI mixtures, TG treatment converted myosin heavy chain and actin into lower molecular-weight polypeptides. A reduced intensity in the electrophoretic bands of soy proteins （7/S and 11S except the basic subunits） was observed in all treatments, suggesting crosslinking with MPI.
出处
《江苏农业学报》
CSCD
北大核心
2005年第3期185-190,共6页
Jiangsu Journal of Agricultural Sciences
基金
江苏省"十五"攻关项目(BE2001400)
关键词
热处理温度
转谷氯酰胺酶
肌原纤维蛋白
大豆分离蛋白
凝胶性
heat treatment temperature
transglutaminase
myofibrillar proteins
soy protein isolates
gelation
