DOI QR코드

DOI QR Code

Effect of Transglutaminase Addition on the Physicochemical Properties of Sodium Caseinate and Whey Proteins

  • Jeong, Ji-Eun (Department of Food and Nutrition, College of Human Ecology. Human Ecology Research Institute, Chonnam National University) ;
  • Hong, Youn-Ho (Department of Food and Nutrition, College of Human Ecology. Human Ecology Research Institute, Chonnam National University)
  • Published : 2009.08.31

Abstract

In this study, several factors were analyzed in an effort to determine the effects of transglutaminase (TGase) treatment on sodium caseinate (NaCN), ${\alpha}--lactalbumin$ (${\alpha}-La$), and ${\beta}-lactoglobulin$ (${\beta}-Lg$) polymerization reactions. The results of SDSPAGE showed that NaCN was slightly hydrolyzed to molecular weights of 50-400 kDa according to activation time. ${\alpha}-La$ formed high-molecular polymers of 30-300 kDa, whereas ${\beta}-Lg$ remained almost completely unhydrolyzed. Melting temperatures of NaCN, ${\alpha}-La$ with and without TGase were all in the range of $100{\pm}10^{\circ}C$ under the endothermic curve, and the melting temperature of ${\beta}-Lg$ with TGase was lower than that with TGase. When the proteins were incubated for 3 h with TGase, the micrographic structures showed a small quantity of sediment and broad layers. The final ${\alpha}-La$ residues remained at a level of 21.38%, and the TGase-treated ${\alpha}-La$ was confirmed to have undergone a profound loss of mass, to 18.25%. The DPPH-radical scavenging activity of NaCN and ${\beta}-Lg$ with TGase treatment was higher than that observed in the untreated sample, while those of ${\alpha}-La$ increased with concentration.

Keywords

References

  1. Aboumahmoud, R. and Savello, P. (1990) Crosslinking of whey protein by transglutaminase. J. Dairy Sci. 73, 256-263 https://doi.org/10.3168/jds.S0022-0302(90)78668-7
  2. Anderson, M. E. (1998) Glutathione: an overview of biosynthesis and modulation. Chemico-Biological Interactions. Archives Biochem. Biophys. 321, 6-12 https://doi.org/10.1006/abbi.1995.1361
  3. Ando, H., Adachi, M., Umeda, K., Matsuura, A., Nonaka, M., Uchio, R., Tanaka, H., and Motoki, M. (1989) Purification and characteristics of a novel transglutaminase derived from microorganisms. Agric. Biol. Chem. 53, 2613-2617 https://doi.org/10.1271/bbb1961.53.2613
  4. Blois, M. S. (1958) Antioxidant determination by the use of a stable free radical. Nature 181, 1199-1200 https://doi.org/10.1038/1811199a0
  5. Bonisch, M. P., Heidebach, T. C., and Kulozik, U. (2008) Influ- ence of transglutaminase protein cross-linking on the rennet coagulation of casein. Food Hydrocolloids 22, 288-297 https://doi.org/10.1016/j.foodhyd.2006.11.015
  6. Boye, J. I. and Alli, I. (2000) Thermal denaturation of mixtures of α-lactalbumin and β-lactoglobulin: A differential scanning calorimetric study. Food Res. Int. 33, 673-682 https://doi.org/10.1016/S0963-9969(00)00112-5
  7. Faergemand, M., Otte, J., and Qvist, K. B. (1997) Enzymatic cross-linking of whey proteins by a $Ca^{2+}$-independent microbial transglutaminase from Streptomyces lydicus. Food Hydrocolloids 11, 19-25 https://doi.org/10.1016/S0268-005X(97)80006-9
  8. Fitzsimons, S. M., Mulvihill, D. M., and Morris, E. R. (2007) Denaturation and aggregation processes in thermal gelation of whey proteins resolved by differential scanning calorimetry. Food Hydrocolloids 21, 638-644 https://doi.org/10.1016/j.foodhyd.2006.07.007
  9. Gu, Y. S., Matsumura, Y., Yamaguchi, S., and Mori, T. (2001) Action of protein-glutaminase on $\alpha$-lactalbumin in the native and molten globule states. J. Agric. Food Chem. 49, 5999-6005 https://doi.org/10.1021/jf010287z
  10. Hwang, J. S., Lee, H. C., and Chin, G. B. (2008) Rheological properties of pork myofibrillar protein and sodium caseinate mixture as affected by transglutaminase with various incubation temperatures and times. Korean J. Food Sci. Animal Resour. 28 (2), 154-159 https://doi.org/10.5851/kosfa.2008.28.2.154
  11. Ikura, K., Kometani, T., Yoshikawa, M., Sasaki, R., and Chiba, H. (1980) Crosslinking of casein components by transglutaminase. Agric. Biol. Chem. 44, 1567-1573 https://doi.org/10.1271/bbb1961.44.1567
  12. Jeong, J. E. and Hong, Y. H. (2005) Properties of Transglutaminase treated milk product powders. Kor. J. Food Sci. Technol. 37, 345-351
  13. Jeong, J. E. and Hong, Y. H. (2006) Electrophoretical properties of transglutaminase treated milk product powders. Kor. J. Food Sci. Technol. 38, 304-308
  14. Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685 https://doi.org/10.1038/227680a0
  15. Lee, D. S., Matsumoto, S., Matsumura, Y., and Mori, T. (2002) Identification of the $\epsilon-\gamma$ (glutamyl) lysine crosslinking site in α-lactalbumin polymerized by mammalian and microbial transglutaminases. J. Agric. Food Chem. 50, 7412-7419 https://doi.org/10.1021/jf020529a
  16. Lee, H. C. and Chin, G. B. (2009) Effect of transglutaminase, acorn, and mungbean powder on quality characteristics of low-fat/salt pork model sausages. Korean J. Food Sci. Animal Resour. 29, 374-381 https://doi.org/10.5851/kosfa.2009.29.3.374
  17. Mahmound, R. and Savello, P. A. (1992) Mechanical properties and water vapor transferability through whey protein films. J. Dairy Sci. 75, 942-946 https://doi.org/10.3168/jds.S0022-0302(92)77834-5
  18. Moon, J. H. and Hong, Y. H. (2003) Electron microscopical property of transglutaminase added milk. Korean J. Food Sci. Animal Resour. 23, 350-355
  19. Nieuwenhuisen, W. F., Dekker, H. L., De, K. L., Groneveld, T., De, K. C. G., and De, J. G. A. (2003) Modification of glutamine and lysine residues in holo and apo α-lactalbumin with microbial transglutaminase. J. Agric. Food Chem. 51, 7132-7139 https://doi.org/10.1021/jf0300644
  20. Nonaka, M., Matsumura, Y., and Motoki, M. (1996) Incorporation of lysine- and lysine dipeptides into $\alpha{s}_1$-casein by $Ca^{2+}$-independent Microbial transglutaminase. Biosci. Biotechnol. Biochem. 60, 131-133 https://doi.org/10.1271/bbb.60.131
  21. Nonaka, M., Toiguchi, S., Sakamoto, H., Kawajiri, H., Soeda, T., and Motoki, M. (1994) Changes caused by microbial transglutaminase on physical properties of thermally induced soy protein gels. Food Hydrocolloids 8, 1-8 https://doi.org/10.1016/S0268-005X(09)80139-2
  22. O'Sullivan, M. M., Kelly, A. L., and Fox, P. F. (2002) Influence of trans- glutaminase treatment on some physico-chemical properties of milk. J. Dairy Res. 69, 433-442 https://doi.org/10.1017/S0022029902005617
  23. Ozer, B., Kirmaci, H.A., Oztekin, S., Hayaloglu, A., and Atamer, M (2007) Incorporation of microfical transglutaminase into non-fat yogurt production. Int. Dairy J. 17, 199-207 https://doi.org/10.1016/j.idairyj.2006.02.007
  24. Partanen, R., Autio, K., Myllarinen, P., Lille, M., Buchert, J., and Forssell, P. (2008) Effect of transglutaminase on structure and syneresis of neutral and acidic sodium caseinate gels. Int. Dairy J. 18, 414-421 https://doi.org/10.1016/j.idairyj.2007.10.002
  25. Sakamoto, H., Kumizawa, Y., and Motoki, M. (1994) Strength of protein gels prepared with microbial transglutaminase as related to reaction conditions. J. Food Sci. 59, 866-871 https://doi.org/10.1111/j.1365-2621.1994.tb08146.x
  26. Sharma, R., Zakora, M., and Qvist, K. B. (2002) Susceptibility of an industrial α-lactalbumin concentrate to cross-linking by microbial transglutaminase. Int. Dairy J. 12, 1005-1012 https://doi.org/10.1016/S0958-6946(02)00122-X
  27. Spellman, E., McEvoy, G., O'Cuinn, R., and FitzGerald, J. (2003) Proteinase and exopeptidase hydrolysis of whey protein: Comparison of the TNBS, OPA and pH stat methods for quantification of degree of hydrolysis. Int. Dairy J. 13, 447-453 https://doi.org/10.1016/S0958-6946(03)00053-0
  28. Traore, F. and Meunier, J. (1991) Cross-linking of caseins by human placental factor X IIIa. J. Agric. Food Chem. 39, 1892-1896 https://doi.org/10.1021/jf00010a042

Cited by

  1. Effects of Bovine α-Lactalbumin Added with Oleic Acid and Microbial Transglutaminase on Cancer Cell Apoptosis vol.41, pp.3, 2012, https://doi.org/10.3746/jkfn.2012.41.3.310