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
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