Excessive cross-linking of caseins by microbial transglutaminase and its impact on physical properties of acidified milk gels

International Dairy Journal

Volumn 20, Issue 5, 2010, Pages 321-327

  Jaros, Doris ^a   Jacob, Mandy ^a   Otto, Clemens ^a   Rohm, Harald ^a  

^a DRESDEN UNIVERSITY OF TECHNOLOGY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CROSS-LINKED PROTEINS; CROSS-LINKING INTENSITY; ENZYME INACTIVATION; MICROBIAL TRANSGLUTAMINASE; MILK GELS; MILK PROTEIN; OLIGOMERISATION; RAW MILK; STERIC HINDRANCES; WEAK GEL;

CASEIN; COAGULATION; GELATION; HEATING; OLIGOMERIZATION;

GELS;

EID: 76749093576     PISSN: 09586946     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.idairyj.2009.11.021     Document Type: Article

References (34)

1. Anema S.G., Lauber S., Lee S.K., Henle T., and Klostermeyer H. Rheological properties of acid gels prepared from pressure and transglutaminase-treated skim milk. Food Hydrocolloids 19 (2005) 879-887
2. Benjakul S., and Visessanguanb W. Transglutaminase-mediated setting in big eye snapper surimi. Food Research International 36 (2003) 253-266
3. Bönisch M.P., Huss M., Weitl K., and Kulozik U. Transglutaminase cross-linking of milk proteins and impact on yoghurt gel properties. International Dairy Journal 17 (2007) 1360-1371
4. Buchert J., Selinheimo E., Kruus K., Mattinen M.-L., Lantto R., and Autio K. Using crosslinking enzymes to improve textural and other properties of food. In: Rastall R. (Ed). Novel enzyme technology for food applications (2007), Woodhead Publishing Ltd., Cambridge, UK 101-139
5. Eissa A.S., and Khan S.A. Modulation of hydrophobic interactions in denatured whey proteins by transglutaminase enzyme. Food Hydrocolloids 20 (2005) 543-547
6. Folk J.E., and Cole P.W. Mechanism of action of guinea pig liver transglutaminase. I. Purification and properties of the enzyme; identification of a functional cysteine essential for activity. Journal of Biological Chemistry 241 (1966) 5518-5525
7. Halim D., Caron K., and Keillor J.W. Synthesis and evaluation of peptidic maleimides as transglutaminase inhibitors. Bioorganic & Medicinal Chemistry Letters 17 (2007) 305-308
8. Horne D.S. Casein interactions: casting light on the black boxes, the structure in dairy products. International Dairy Journal 8 (1998) 171-177
9. Horne D.S. Casein micelles as hard spheres: limitations of the model in acidified gel formation. Colloids and Surfaces A: Physicochemical and Engineering Aspects 213 (2003) 255-263
10. Huppertz T., and de Kruif C.G. Ethanol stability of casein micelles cross-linked with transglutaminase. International Dairy Journal 17 (2006) 436-441
11. Huppertz T., and de Kruif C.G. Rennet-induced coagulation of enzymatically cross-linked casein micelles. International Dairy Journal 17 (2006) 442-447
12. IDF. Determination of the casein content of milk. IDF Standard 29 (1964), International Dairy Federation, Brussels, Belgium
13. IDF. Milk - Determination of fat content - Gerber butyrometers. IDF Standard 51 (1982), International Dairy Federation, Brussels, Belgium
14. IDF. Milk - Determination of nitrogen content - part 1: Kjeldahl method. IDF Standard 20-1 (2001), International Dairy Federation, Brussels, Belgium
15. Jaros D., Heidig C., and Rohm H. Enzymatic modification through microbial transglutaminase enhances the viscosity of stirred yogurt. Journal of Texture Studies 38 (2007) 179-198
16. Jaros D., Partschefeld C., Henle T., and Rohm H. Transglutaminase in dairy products: chemistry, physics, applications. Journal of Texture Studies 37 (2006) 113-155
17. Jaros D., Pätzold J., Schwarzenbolz U., and Rohm H. Small and large deformation rheology of acid gels from transglutaminase treated milks. Food Biophysics 1 (2006) 124-132
18. de Jong G.A.H., and Koppelman S.J. Transglutaminase catalyzed reactions: impact on food applications. Journal of Food Science 67 (2002) 2798-2806
19. Kanaji T., Ozaki H., Takao T., Kawajiri H., Ide H., Motoki M., et al. Primary structure of microbial transglutaminase from Streptoverticillium sp. strain s-8112. Journal of Biological Chemistry 268 (1993) 11565-11572
20. Labuza T.P., and Altunakar B. Water activity prediction and moisture sorption isotherms. In: Barbosa-Canovas G.V., Fontana A.J., Schmidt S.J., and Labuza T.P. (Eds). Water activity in foods (2007), Blackwell Publishing Ltd, Oxford, UK 109-154
21. Lakemond C.M.M., and van Vliet T. Acid skim milk gels: the gelation process as affected by preheating pH. International Dairy Journal 18 (2008) 574-584
22. Lauber S., Henle T., and Klostermeyer H. Relationship between the crosslinking of caseins by transglutaminase and the gel strength of yoghurt. European Food Research and Technology 210 (2000) 305-309
23. Lee D.-S., Matsumoto S., and Matsumura Y. Identification of the ε-(γ-glutamyl)lysine cross-linking sites in α-lactalbumin polymerized by mammalian and microbial transglutaminases. Journal of Agricultural and Food Chemistry 50 (2002) 7412-7419
24. Lorenzen P.C., Neve H., Mautner A., and Schlimme E. Effect of enzymatic cross-linking of milk proteins on functional properties of set-style yoghurt. International Journal of Dairy Technology 55 (2002) 152-157
25. Lorenzen P.C., Schrader K., Einhoff K., and Rohenkohl H. Einfluss der enzymatischen Quervernetzung von Milcheiweiß auf die Eigenschaften gerührter Joghurt- und Dickmilcherzeugnisse. Kieler Milchwirtschaftliche Forschungsberichte 57 (2005) 97-115
26. Moreno H.M., Carballo J., and Borderias A.J. Study of two different cold restructuring processes using two different qualities of hake (Merluccius capensis) muscle, with addition of microbial transglutaminase. Journal of the Science of Food and Agriculture 89 (2008) 136-1351
27. Schey, A. (2003). Texture improvement of fermented dairy products by crosslinking with transglutaminase. In Proceedings of the IDF-seminar on aroma and texture of fermented milk (pp. 371-375). Kolding, Denmark.
28. Schorsch C., Carrie H., and Norton I.T. Cross-linking casein micelles by a microbial transglutaminase: influence of cross-links in acid-induced gelation. International Dairy Journal 10 (2000) 529-539
29. Sharma R., Lorenzen P.C., and Qvist K.B. Influence of transglutaminase treatment of skim milk on the formation of ε-(γ-glutamyl)lysine and the susceptibility of individual proteins towards crosslinking. International Dairy Journal 11 (2001) 785-793
30. Stangierski J., and Baranowska H.M. Analysis of texture and dynamics of water binding in enzymatically modified myofibrillar preparation obtained from washed mechanically recovered poultry meat. European Food Research and Technology 226 (2008) 857-860
31. Tang C., Yang X.Q., Chen Z., Wu H., and Peng Z.Y. Physicochemical and structural characteristics of sodium caseinate biopolymers induced by microbial transglutaminase. Journal of Food Biochemistry 29 (2005) 402-421
32. Truong V.-D., Clare D.A., Catignani G.L., and Swaisgood H.E. Cross-linking and rheological changes of whey proteins treated with microbial transglutaminase. Journal of Agricultural and Food Chemistry 52 (2004) 1170-1176
33. Vasbinder A.J., Rollema H.S., Bot A., and de Kruif C.G. Gelation mechanism of milk as influenced by temperature and pH: studied by the use of transglutaminase cross-linked casein micelles. Journal of Dairy Science 86 (2003) 1556-1563
34. Worratao A., and Yongsawatdigul J. Purification and characterization of transglutaminase from Tropical tilapia (Oreochromis niloticus). Food Chemistry 93 (2005) 651-658