Properties of Transglutaminase Treated Milk Product Powders

Transglutaminase를 처리한 분말 유제품의 특성

  • Jeong, Ji-Eun (Department of Food and Nutrition, Chonnam Natioinal University.Human Ecology Research Institute.BioFood Research Center) ;
  • Hong, Youn-Ho (Department of Food and Nutrition, Chonnam Natioinal University.Human Ecology Research Institute.BioFood Research Center)
  • 정지은 (전남대학교 식품영양학과.생활과학연구소.바이오식품연구센터) ;
  • 홍윤호 (전남대학교 식품영양학과.생활과학연구소.바이오식품연구센터)
  • Published : 2005.06.30


Physicochemical properties and functionalities of sodium caseinate, whey protein, skim milk, and whole milk with or without transglutaminase (TGase, 200 : 1) at $38^{\circ}C$ were determined. After crosslinking by TGase, whey protein was effective in improving heat stability compared to native protein at over $70^{\circ}C$. Whole milk was stable with lower turbidity compared to native solution. Whey protein showed low hydrolysis degree, fewer than sodium caseinate, during early activation time and increased slightly thereafter Emulsifying activities of sodium caseinate at pH 2 and 8, and whey protein at pH 7 and 8 improved. Emulsion stability of sodium caseinate improved at entire pH range studied. Foam expansion and foam stability of samples improved with TGase-treatment. Viscosities of TGase-treated samples were higher than those of untreated ones.


transglutaminase;cross-linking;sodium caseinate;whey protein


  1. Motoki M, Nio N. Crosslinking between different food proteins by transglutaminase. J. Food Sci. 48: 561-566 (1983)
  2. Flanagan J, Gunning Y, FitzGerald RJ. Effect of cross-linking with transglutaminase on the heat stability and some functional characteristics of sodium caseinate. Food Res. Intl. 36: 267-274 (2003)
  3. Slattery H, FitzGerald RJ. Functional properties and bitterness of sodium caseinate hydrolysates prepared with a Bacillus proteinase. J. Food Sci. 63: 418-422 (2003)
  4. Patel MA, Kilara A. Studies on whey protein concentrate. Foaming and emulsifying properties and their relationships with physi-cochemical properties. J. Dairy Sci. 73: 2731-2740 (1990)
  5. Motoki M, Segura K. Transglutaminase and its uses for food processing. Trends Food Sci. Technol. 9: 204-210 (1998)
  6. Imm JY. Functional properties of transglutaminase treated and processed skim milk powder, pp. 81-88 In: 50th spring symposium. May 19, Konkuk Univ., Seoul, Korea. Korean Dairy Technol. Sci. Assoc, Seoul, Korea (2000)
  7. Faergemand M, Otte J, Qvist KB. Emulsifying properties proteins cross-linked with microbial transglutaminase. Intl. Dairy J. 8: 715-723(1998)
  8. James CS. Analytical Chemistry of Foods. Blackie Academic and Professional, Glasgow, UK. pp. 130-131 (1995)
  9. Babiker EFE, Khan MAS, Matsudomi N, Kato A. Polymerization of soy protein digests by microbial transglutaminase for improvement of the functional properties. Can. Food Sci. Technol. 29: 627-634 (2000)
  10. De Wit JH. Functional properties of whey protein, pp. 258-321 In: Developments in Dairy Chemistry, Series 4. Elsevier Applied Sci. London, UK (1989)
  11. Lowry OH, Rosebrough NJ, Farr AL, Randall RT. Protein measurement with the folin phenol reagent. J. Biol. Chem. 193: 265-275(1951)
  12. Lorenzen PC. Techno-functionalproperties of transglutaminase-treated milk protein. Milchwiss. 55: 667-670 (2000)
  13. Kato Y, Aoki T, Kato N, Nakamura R, Matsuda T. Modification of ovalbumin with glucose 6-phosphate by amino-carbonyl reaction. Improvement of protein heat stability and emulsifying activity. J. Agric. Food Chem. 43: 301-305 (1995)
  14. Nonaka M, Matsumura Y, Motoki M. Incorporation of lysine and lysine dipeptides into ${\alpha}_{s1}-casein$ by $ca^{2+}-independent$ microbial transglutaminase. Biosci. Biotech. Biochem. 60: 131-133 (1996)
  15. Folch J, Lees M, Slane GH. A simple method for the isolation and purification for total lipides from animal tissues. J. Biol. Chem. 193: 183-191 (1951)
  16. Sakamoto H, Kumazawa Y, Motoki M. Strength of protein gels prepared with microbial transglutaminase as related to reaction conditions. J. Food Sci. 59: 866-871 (1994)