Title of article :
NOTE: Identification of Wheat Protein Components Involved in Polymer Formation on Incubation with Transglutaminase.
Author/Authors :
Mujoo، . نويسنده , , Ng، P. K. W. نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2003
Pages :
-702
From page :
703
To page :
0
Abstract :
Transglutaminase (TG) catalyzes acyl-transfer reactions, introducing covalent cross-links between L-lysine and L-glutamine residues. As a result, peptides are connected and the structure of a stabilized protein network is formed, thereby improving protein strength. In this study, wheat flour was incubated with TG for different time intervals (0, 30, 60, 120, and 240 min) and the extent of polymer formation and proteins involved were investigated by SE-HPLC, SDS-PAGE, and RP-HPLC. Results indicated that the amount of polymers formed increased with incubation time. TG induced the cross-linking of HMW glutenin subunits more so than of other proteins in wheat
Keywords :
Cocos nucifera , peat substitutes , container media , waste-grade coir , Sustainable Agriculture , waste reclamation
Journal title :
CEREAL CHEMISTRY
Serial Year :
2003
Journal title :
CEREAL CHEMISTRY
Record number :
78492
Link To Document :
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