Browse > Article

Emulsifying Properties of Whey Protein Hydrolysates  

양희진 (성균관대학교 식품·생명자원학과)
이수원 (성균관대학교 식품·생명자원학과)
Publication Information
Food Science of Animal Resources / v.23, no.1, 2003 , pp. 63-69 More about this Journal
Abstract
This experiment was carried out to study changes in solubility and emulsifying properties of whey protein. Whey protein hydrolysates were obtained from tryptic hydrolysis of whey protein concentrate at pH 8.0 and 37$^{\circ}C$ for 6 hours. Emulsifying activity of whey protein hydrolysate was highest at 4 hours of hydroysis and at 5.50% of DH. During hydrolysis of whey protein concentrate with trypsin, ${\alpha}$-lactalbumin was not easily broken down. But ${\beta}$-lactoglobulin was hydrolysed rapidly from the early stage of hydrolysis, producing several low molecular weight peptides, which have to participate in increasing emusifying activity. The solulbility of hydyolysates tended to increase depending on hydrolysis time; however, there was a gradual decrease after 5 hours. The hydrolysate had a minimum solubility near the isoelectric point range (pH 4∼5). The more hydrolysed the whey protein concentrates, the more soluble they are near the pl. They aye also more soluble above pH 6. Emulsifying activity of hydrolysates showed similar results to solubility. Creaming stability gradually increased when hydrolysis increased, increasing rapidly above pH 8 after 4 hours of hydrolysis.
Keywords
whey protein concentrates; hydrolysates; emulsifying activity; solubility; creaming stability;
Citations & Related Records
연도 인용수 순위
  • Reference
1 Adler-Nissen, J. (1976) Enzymatic hydrolysis of proteins for increased solubility. J. Agric. Food Chem. 24, 1090-1093   DOI   PUBMED
2 Britten, M., Giroux, H. J., and Gaudin, V. (1994) Effect of pH during heat processing of partially hydrolyzed whey protein. J. Dairy Sci. 11, 676-84
3 Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227, 680-685   DOI   PUBMED   ScienceOn
4 Shimizu, M., Lee, S. W., Kaminogawa, S., and Yamauch, K. (1986) Functional properties of a peptide of $\alpha_{s1}$-casein : changes in the emulsifying activity during purification of the peptide. J. Food Sci. 51 1248-1252   DOI
5 Chobert, J. M., Bertrand-Herb, C., and Nicolas, M. G. (1988a) Solubility and emulsifying properties of caseins and whey proteins modified enzymatically by trypsin. J. Asric. Food Chem. 36, 883-892   DOI
6 AdIer-.Nissen, J., Eriksen, S., and Olsen, H. S. (1983) Improvement of the functionality of vegetable proteins by controlled enzymatic hydrolysis. In Plant proteins for human food ; Bodwell, C. E. and Petit, L., Nijhoff, M., and Junk, W. (eds.), The Hague., PP. 207- 219
7 Fox, P. F., Morrissey, P. A., and Mulvihill, D. M. (1982) Chemical and enzymatic modification of food proteins. In Developments in Food Proteins-l. Hudson, B. J. F.(ed.), Applied Science, London, pp. 1-.60
8 De Wit, J. N. and Klarenbeek, G. (1984) Effect of various heat treatments of structure and solubility of whey proteins. J. Dairy Sci. 67, 2701-2711   DOI
9 Olsen, H. S. and Adler-Nissen, J. (1979) Industrial production and applications of a soluble enzymatic hydrolyzate of soya protcin. Process Biochem. 14, 6-11
10 Ribadeau-Dumas, B. (1988) Structure and variability of milk proteins. In Mitk proteins: nutritional, clinical, functional and techtiolosical aspects. Barth, C. A. and Schilmme, E.(ed.), Sprin-ger Verlag, New York
11 Bertrand-Harb, C., Baday, A., Dalgalarrondo, M., Chobert, J. M., and Haertle, T. (2002) Thermal modifications of structure and co-denaturation of $\alpha$ -lactalbumin and $\beta$-lactoglobulin inducechanges of solubility and susceptibility to proteases. Nahrune. 46,283-289   DOI   ScienceOn
12 Pearce, N. K. and Kinsella, J. E. (1978) Emulsifying properties of proteins : Evalution of a turbidimetric technique. J. Agric. Food Chem. 26, 716-723   DOI
13 Chobert, J. M., Sitohy, M. Z., and Whitaker, J. R. (1988b)Solubility and emulsifying properties of caseins modified enzy-matically by Staphylococcus aureus V8 protease. J. Asric. Food Chem. 36, 220-224   DOI
14 Alder-Nissen, J. (1986) Enzymic hydrolysis of food proteins. Elsevier Applied Science Publishers. New York
15 Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. S. (1951) Protein measurement with the folin phenol reagent. J. Binl. Chem. 193, 265-275
16 Alder-Nissen, J. (1979) Determination of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid. J. Agric. Food Chem. 27, 1256-1261   DOI   PUBMED
17 Adler-Nissen, J. and Olsen, H. S. (1979) In Functionatity and protein structure. Pour-El. (ed). Advances in Chemistry Series 92, American Chemical Society, Washington D.C., PP. 125-146
18 Lee, S. W. and Kim, J. W. (1992) Effect of enzymatic hydrolysis on emulsifying properties of casein. Korean J. Dairy Sci. 14, 184-191