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《Jiangsu Journal of Agricultural Sciences》 2005-03
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Effects of Transglutaminase on Gelation of Protein Mixtures at Different Heat Treatment Temperatures

ZU Hai-zhen, XU Xing-lian, LU Yi-jun, ZHOU Guang-hong (Key Laboratory of Agricultural and Animal Products Processing and Quality Control, Ministry of Agricultrue, Nanjing Agricultural University, Nanjing 210095, China)  
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 glycinin, 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 (7S and 11S except the basic subunits) was observed in all treatments, suggesting cross-linking with MPI.
【Fund】: 江苏省“十五”攻关项目(BE2001400)
【CateGory Index】: TS251.1
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