Advanced SearchSearch Tips
Calcium-binding Peptides Derived from Tryptic Hydrolysates of Cheese Whey Protein
facebook(new window)  Pirnt(new window) E-mail(new window) Excel Download
 Title & Authors
Calcium-binding Peptides Derived from Tryptic Hydrolysates of Cheese Whey Protein
Kim, S.B.; Lim, J.W.;
  PDF(new window)
The purpose of this research was to investigate the potential use of cheese whey protein (CWP), a cheese by-product. The physiological activity of calcium-binding peptides in CWP may be used as a food additive that prevents bone disorders. This research also examined the characteristics of calcium-binding peptides. After the CWP was heat treated, it was hydrolyzed by trypsin. Then calcium-binding peptides were separated and purified by ion-exchange chromatography and reverse phase HPLC, respectively. To examine the characteristics of the purified calcium-binding peptides, amino acid composition and amino acid sequence were analyzed. Calcium-binding peptides with a small molecular weight of about 1.4 to 3.4 kDa were identified in the fraction that was flowed out from 0.25 M NaCl step gradient by ion-exchange chromatography of tryptic hydrolysates. The results of the amino acid analysis revealed that glutamic acid in a calcium-binding site took up most part of the amino acids including a quantity of proline, leucine and lysine. The amino acid sequence of calcium-binding peptides showed Phe-Leu-Asp-Asp-Asp-Leu-Thr-Asp and Ile-Leu-Asp-Lys from -LA and Ile-Pro-Ala-Val-Phe-Lys and Val-Tyr-Val-Glu-Glu-Leu-Lys from -LG.
Cheese Whey Protein;Calcium-binding Peptide;Tryptic Hydrolysate;
 Cited by
유청단백질의 분리 및 단백질 분해 효소에 의한 유청단백질의 가수분해 양상,렌친핸드;배형철;정석근;남명수;

농업과학연구, 2012. vol.39. 4, pp.561-568 crossref(new window)
Enzymatic Hydrolysis of Heated Whey: Iron-Binding Ability of Peptides and Antigenic Protein Fractions, Journal of Dairy Science, 2007, 90, 9, 4033  crossref(new windwow)
Review of in vitro digestion models for rapid screening of emulsion-based systems, Food & Function, 2010, 1, 1, 32  crossref(new windwow)
Calcium Binding Peptide Motifs from Calmodulin Confer Divalent Ion Selectivity to Elastin-Like Polypeptides, Biomacromolecules, 2013, 14, 7, 2347  crossref(new windwow)
Novel Peptide with a Specific Calcium-Binding Capacity from Whey Protein Hydrolysate and the Possible Chelating Mode, Journal of Agricultural and Food Chemistry, 2014, 62, 42, 10274  crossref(new windwow)
Preparation, characterization and identification of calcium-chelating Atlantic salmon (Salmo salar L.) ossein oligopeptides, European Food Research and Technology, 2015, 241, 6, 851  crossref(new windwow)
Purification and characterisation of a glutamic acid-containing peptide with calcium-binding capacity from whey protein hydrolysate, Journal of Dairy Research, 2015, 82, 01, 29  crossref(new windwow)
Effects of Calcium-Binding Peptide from Tilapia Scale Protein Hydrolysates on Calcium Absorption in Caco-2 Cells, Journal of Aquatic Food Product Technology, 2016, 25, 8, 1213  crossref(new windwow)
Bioactive Peptides Isolated from Casein Phosphopeptides Enhance Calcium and Magnesium Uptake in Caco-2 Cell Monolayers, Journal of Agricultural and Food Chemistry, 2017, 65, 11, 2307  crossref(new windwow)
Adamson, N. J. and E. C. Reynolds. 1996. Characterization of casein phosphopeptides prepared using alcalase: Determination of enzyme specificity. Enzyme Microb. Tech. 19:202-207.

Anderson, P. J., C. L. Brooks and L. J. Berliner. 1997. Functional identification of calcium binding residues in bovine $\alpha$- lactalbumin. Biochemistry. 36:11648-11654.

AOAC. 1990. Official Methods of Analysis. 15th edn. Association of Official Analytical Chemists, Arlington, Verginia.

Avioli, L. V. 1984. Calcium and osteoporosis. Annu. Rev. Nutr. 4:471-491. crossref(new window)

Bennett, T., A. Desmond, M. Harrington, D. McDonagh, R. FitzGerald, A. Flynn and K. D. Cashman. 2000. The effect of high intakes of casein and casein phosphopeptide on calcium absorption in the rat. Br. J. Nutr. 83:673-680.

Bradford, M. M. 1976. A rapid and sensitive methods for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254. crossref(new window)

Feng, M., L. van der Does and A. Bantjes. 1995. Preparation of apo-lactoferrin with a very low iron saturation. J. Dairy Sci. 78:2352-2357.

Friedlander, E. J. and A. W. Norman. 1980. Purification of chick intestinal calcium binding protein. Methods Enzymol. 67:504-508.

Fullmer, C. S. and R. H. Wasserman. 1981. The amino acid sequence of bovine intestinal calcium-binding protein. J. Biol. Chem. 256:5669-5674.

Harwalkar, V. R. and D. J. McMahon. 1993. Symposium: Biological and food functional characterizations of milk protein hydrolysis products. J. Dairy Sci. 76:300.

Hiraoka, Y., T. Segawa, K. Kuwajima, S. Sugai and N. Murai. 1980. $\alpha$-Lactalbumin: A calcium metalloprotein. Biochem. Biophys. Res. Commun. 95:1098-1104.

Jeyarajah, S. and J. C. Allen. 1994. Calcium binding and saltinduced structural changes of native and preheated$\beta$- lactoglobulin. J. Agric. Food Chem. 42:80-85.

Kim, S. B., H. S. Shin and J. W. Lim. 2004. Separation of calciumbinding protein derived from enzymatic hydrolysates of cheese whey protein. Asian-Aust. J. Anim. Sci. 17:712-718.

Kitts, D. D. and Y. V. Yuan. 1992. Caseinophosphopeptides and calcium bioavailability. Trends Food Sci. Tech. 3:31-35.

Kosikowski, F. 1982. Cheese and fermented milk foods. 2nd ed. Edward Brothers Inc., Michigan, USA.

Lipkin, M. and H. Newmark. 1985. Effect of added dietary calcium on colonic epithelial-cell proliferation in subjects at high risk for familial colonic cancer. New England J. Med. 313:1381-1384.

Moore, S., D. H. Spackman and W. H. Stein. 1958. Automatic recording apparatus for use in the chromatography of amino acids. Fed. Proc. 17:1107-1115.

Nemirovskiy, O. V. and M. L. Gross. 2000. Intrinsic Ca2+ affinities of peptides: Application of the kinetic method to analogs of calcium-binding site III of rabbit skeletal troponin C. J. Am. Soc. Mass Spectrom. 11:770-779.

Noyelle, K. and H. van Dael. 2002. Kinetics of conformational changes induced by the binding of various metal ions to bovine $\alpha$-lactalbumin. J. Inorg. Biochem. 88:69-76.

Osborne, C. G., R. B. Mc Tyre, J. Dudek, K. E. Roche, R. Scheuplein, B. Silverstein, M. S. Weinberg and A. A. Salkeld. 1996. Evidence for the relationship of calcium to blood pressure. Nutr. Rev. 54:365-381.

Permyakov, E. A., V. V. Yarmolenko, L. P. Kalinichenko, L. A. Morozova and E. A. Burstein. 1981. Calcium binding to alphalactalbumin: Structural rearrangement and association constant evaluation by means of intrinsic protein fluorescence changes. Biochem. Biophys. Res. Commun. 100:191-197.

Pintado, M. E., A. E. Pintado and F. X. Malcata. 1999. Controlled whey protein hydrolysis using two alternative protease. J. Food Eng. 42:1-13.

Renner, E. 1994. Dairy calcium, bone metabolism and prevention of osteoporosis. J. Dairy Sci. 77:3498-3505.

Reynolds, E. C. 1997. Remineralization of enamel subsurface lesions by casein phosphopeptide-stabilized calcium phosphate solutions. J. Dent. Res. 76:1587-1595. crossref(new window)

Rose, D., D. T. Davies and M. Yaguchi. 1969. Quantitative determination of the major components of casein mixture by column chromatography on DEAE-cellulose. J. Dairy Sci. 52:8-11.

Schagger, H. and G. von Jagow. 1987. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166:368-379.

Shaw, D., M. Messer, A. M. Scrivener, K. R. Nicholas and M. Griffiths. 1993. Isolation, partial characterization and amino acid sequence of $\alpha$-lactalbumin from platypus (Ornithorynchus anatinus) milk. Biochem. Biophys. Acta. 1161:177-186.

Spencer, H. and L. Kramer. 1986. NIH consensus conference: osteoporosis. Factors contributing to osteoporosis. J. Nutr. 116:316-319.

Stuart, D. I., K. R. Acharya, N. P. C. Walker, S. G. Smith, M. Lewis and D. C. Phillips. 1986.$\alpha$ -lactalbumin possesses a novel calcium binding loop. Nature (Load). 324:84-87.

Tamura, M., T. Oku and N. Hosoya. 1982. Calcium-binding proteins in bovine milk: Calcium-binding properties and amino acid composition. J. Nutr. Sci. Vitaminol (Tokyo). 28:533-541.

Tuan, R. S., W. A. Scott and Z. A. Cohn. 1978. Purification and characterization of calcium-binding protein from chick chorioallantoic membrane. J. Biol. Chem. 253:1011-1016.

Turgeon, S. L. and S. F. Gauthier. 1990. Whey peptide fractions obtained with a two-step ultrafiltration process: Production and characterization. J. Food Sci. 55:106-110.

Vegarud, G. E., T. Langsrud and C. Svenning. 2000. Mineralbinding milk proteins and peptides; occurrence, biochemical and technological characteristics. Br. J. Nutr. 84:S91-98.

Veprintsev, D. B., M. Narayan, S. E. Permyakov, V. N. Uversky, C. L. Brooks, A. M. Cherskaya, E. A. Permyakov and L. J. Berliner. 1999. Fine tuning the N-terminus of a calcium binding protein: $\alpha$-lactalbumin. Proteins. 37:65-72.

Wang, J. H. and D. M. Waisman. 1979. Calmodulin and its role in the second-messenger system. Curr. Top. Cell. Regul. 15:47-107.

Wasserman, R. H., C. S. Fullmer and A. N. Taylor. 1978. The vitamin D-dependent calcium-binding proteins. In: Vitamin D (Ed. D. E. M. Lawson). Academic Press Inc., NY, USA. 133-166.

Wong, N. P., D. E. LaCroix and F. E. McDonough. 1978. Minerals in whey and whey fractions. J. Dairy Sci. 61:1700-1703.

Kitts, D. D. and Y. V. Yuan. 1992. Caseinophosphopeptides and calcium bioavailability. Trends Food Sci. Tech. 3:31-35.