Korean Journal of Food Science and Technology (한국식품과학회지)

Korean Society of Food Science and Technology (한국식품과학회)
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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
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Abstract

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.

본 연구에서는 시판되고 있는 카제인 나트륨, 유청 단백질, 탈지분유 및 전지분유에 TGase를 첨가하여 이화학적 특성 및 식품첨가물 소재로서의 기능적 특성 등을 조사하였다. 카제인 나트륨의 경우 TGase효소 반응 후 pH 2, pH 4와 알칼리 범위에서, 유청 단백질은 pH 4에서 용해성이 향상되었고 탈지분유에서는 pH 4와 전지분유에서는 모든 pH 범위에서 용해성이 향상되었다. TGase를 첨가한 우유 단백질과 우유 분말 제품이 무첨가군에 비하여 pH 의존적으로 용해성, 유화활성 및 거품형성 등에 기능적 특성이 부분적으로 우수함을 알 수 있었다. 또한 TGase 첨가에 따라 일반성분의 변화가 없었으며 인체내 소화효소에 의해 가수분해가 용이하였고 점도의 증가가 관찰되었다. TGase를 첨가한 제품은 이화학적, pH 및 반응시간 등의 특징에 의하여 영향을 받으므로 식품에 응용할 경우 기능성들이 합리적으로 조절되도록 함이 바람직하다.

Keywords

References

  1. 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)
  2. Motoki M, Segura K. Transglutaminase and its uses for food processing. Trends Food Sci. Technol. 9: 204-210 (1998) https://doi.org/10.1016/S0924-2244(98)00038-7
  3. 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) https://doi.org/10.1271/bbb.60.131
  4. Motoki M, Nio N. Crosslinking between different food proteins by transglutaminase. J. Food Sci. 48: 561-566 (1983) https://doi.org/10.1111/j.1365-2621.1983.tb10790.x
  5. Lowry OH, Rosebrough NJ, Farr AL, Randall RT. Protein measurement with the folin phenol reagent. J. Biol. Chem. 193: 265-275(1951)
  6. 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)
  7. James CS. Analytical Chemistry of Foods. Blackie Academic and Professional, Glasgow, UK. pp. 130-131 (1995)
  8. 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)
  9. 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) https://doi.org/10.1021/jf00050a007
  10. Faergemand M, Otte J, Qvist KB. Emulsifying properties proteins cross-linked with microbial transglutaminase. Intl. Dairy J. 8: 715-723(1998) https://doi.org/10.1016/S0958-6946(98)00111-3
  11. 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) https://doi.org/10.1016/S0963-9969(02)00168-0
  12. Slattery H, FitzGerald RJ. Functional properties and bitterness of sodium caseinate hydrolysates prepared with a Bacillus proteinase. J. Food Sci. 63: 418-422 (2003) https://doi.org/10.1111/j.1365-2621.1998.tb15755.x
  13. Lorenzen PC. Techno-functionalproperties of transglutaminase-treated milk protein. Milchwiss. 55: 667-670 (2000)
  14. De Wit JH. Functional properties of whey protein, pp. 258-321 In: Developments in Dairy Chemistry, Series 4. Elsevier Applied Sci. London, UK (1989)
  15. 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) https://doi.org/10.3168/jds.S0022-0302(90)78958-8
  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) https://doi.org/10.1111/j.1365-2621.1994.tb08146.x