Short communication: Influence of transglutaminase on the heat stability of milk

Journal of Dairy Science

Volumn 84, Issue 6, 2001, Pages 1331-1334

  O'Sullivan, M M ^a   Lorenzen, P C ^b   O'Connell, J E ^a   Kelly, A L ^a   Schlimme, E ^b   Fox, P F ^a  

^a UNIVERSITY COLLEGE CORK   (Ireland)

^b FEDERAL RESEARCH INSTITUTE OF NUTRITION AND FOOD   (Germany)

Author keywords

Heat stability; Milk; Transglutaminase

Indexed keywords

COAGULATING AGENT; MILK PROTEIN; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE;

ANIMAL; ARTICLE; CHEMISTRY; DRUG EFFECT; HEAT; MILK; PH; PHYSIOLOGY; TIME;

ANIMALS; COAGULANTS; HEAT; HYDROGEN-ION CONCENTRATION; MILK; MILK PROTEINS; TIME FACTORS; TRANSGLUTAMINASES;

EID: 0035375266     PISSN: 00220302     EISSN: None     Source Type: Journal    
DOI: 10.3168/jds.S0022-0302(01)70162-2     Document Type: Article

References (19)

1. Davies, D. T., and J.C.D. White. 1966. The stability of milk prior to heat. 1. Subjective measurement of heat stability of milk. J. Dairy Res. 33:67-81.
2. Dickinson, E. 1997. Enzymic crosslinking as a tool for food colloid rheology control and interfacial stabilisation. Trends Food Sci. Technol. 8:334-339.
3. Fox, P. F. 1982. Heat induced coagulation of milk. Pages 189-228 in Developments in Dairy Chemistry. 1. Proteins. P. F. Fox, ed. Elsevier Applied Science Publishers, London, UK.
4. Fox, P. F., and P.L.H. McSweeney. 1998. Dairy Chemistry and Biochemistry. Chapman and Hall, London, UK.
5. Fox, P. F., and P. A. Morrissey. 1977. Reviews on the progress of dairy science: The heat stability of milk. J. Dairy Res. 42:427-435.
6. Han, X-Q., and S. Damodaran. 1996. Thermodynamic compatibility of substrate proteins affects their cross-linking by transglutaminase. J. Agric. Food Chem. 44:1211-1217.
7. Ikura, K., R. Sasaki, and M. Motoki. 1992. Use of transglutaminase in quality improvement and processing of food proteins. Comm. Agric. Food Chem. 2:389-487.
8. Ikura, K., M. Yoshikawa, R. Sasaki, and H. Chiba. 1984. Use of transglutaminase. Reversible blocking of amino groups in substrate proteins for a high yield of specific products. Agric. Biol. Chem. 48:2347-2354.
9. Lorenzen, P. C. 2000. Renneting properties of transglutaminase-treated milk. Milchwissenshaft 55:433-437.
10. Lorenzen, P. C., and E. Schlimme. 1998. Properties and potential fields of application of transglutaminase preparations in dairying. Pages 47-53 in Bull. 332, International Dairy Federation, Brussels, Belgium.
11. McCrae, C. H., and D. D. Muir. 1995. The heat stability of milk. Pages 206-230 in Heat Induced Changes in Milk. Special Issue 9501. P. F. Fox, ed. International Dairy Federation, Brussels, Belgium.
12. Motoki, M., and K. Segura. 1998. Transglutaminase and its uses for food processing. Trends Food Sci. Technol. 9:204-210.
13. Nielsen, P. M. 1995. Reactions and potential industrial applications of transglutaminase. Review of literature and patents. Food Biotechnol. 9:119-156.
14. Nio, N., M. Motoki, and K. Takinami. 1986. Gelation mechanisms of protein solutions by transglutaminase. Agric. Biol. Chem. 48:851-855.
15. 2+-independent transglutaminase derived from microorganism. Agric. Biol. Chem. 53:2619-2623.
16. O'Connell, J. E., and P. F. Fox. 2001. Heat stability of milk and heat induced changes. In Advanced Dairy Chemistry. I. Proteins. 3rd ed. P. F. Fox and P.L.H. McSweeney, ed. Aspen Publications, Gaithersburg, MD, USA. (In press.)
17. Singh, H., and L. K. Creamer. 1992. Heat stability of milk. Pages 621-656 in Advanced Dairy Chemistry. 1. Proteins. P. F. Fox, ed. Elsevier Applied Science Publishers, London, UK.
18. Traore, F., and J. C. Meunier. 1992. Crosslinking activity of placental F XIIIa on whey proteins and caseins. J. Agric. Food Chem. 40:399-402.
19. van Boekel, M.A.J.S., J. A. Nieuwenhuijse, and P. Walstra. 1989. The heat coagulation of milk. 3. Comparison of theory and experiment. Neth. Milk Dairy J. 43:147-162.