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Journal of Dairy Science Vol. 73 No. 2 256-263
© 1990 by American Dairy Science Association ®
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Crosslinking of Whey Protein by Transglutaminase

Reyad Aboumahmoud 1 and Paul Savello 1

1 Department of Nutrition and Food Sciences, Utah State University, Logan 84322-8700

Guinea pig liver transglutaminase (EC 2.3.2.13) was used to enzymically crosslink the whey protein alpha-lactalbumin, ß-lactoglobulin, blends of these protein fractions, whey proteins in powdered whey, and whey proteins in modified powdered whey. Transglutaminase actively crosslinked whey proteins over a wide pH range (6.5 to 8.0). Crosslinking gradually increased with increased incubation time to 4 h. Crosslinking was negligible with transglutaminase after 4 h of incubation. Reconstituted commercial whey and modified whey powders contained sufficient Ca2+ for crosslinking by .92 units transglutaminase/ml of reconstituted whey powder (2% protein) and modified whey powder solutions (1 to 5% protein). Reconstituted whey and modified whey powder (35% protein) served as protein sources for crosslinking by transglutaminase without further adjustment of pH or Ca2+. Dithiothreitol was required to crosslink the whey protein.

Key Words: whey protein • crosslinking • transglutaminase

Submitted on April 26, 1989
Accepted on August 25, 1989




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T. Konno, T. Morii, H. Shimizu, S. Oiki, and K. Ikura
Paradoxical Inhibition of Protein Aggregation and Precipitation by Transglutaminase-catalyzed Intermolecular Cross-linking
J. Biol. Chem., April 29, 2005; 280(17): 17520 - 17525.
[Abstract] [Full Text] [PDF]


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Copyright © 1990 by the American Dairy Science Association ®.