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Casein phosphopeptides

In addition, gelatin peptides have shown to accelerate absorption of dietary calcium in animal models increasing calcium bioavailability (Kim et al., 1998). Jung et al. (2006) reported that fish bone peptides (FBP) could inhibit the formation of insoluble Ca salts in neutral pFI. During the experimental period, Ca retention was increased and loss of bone mineral was decreased by FBP II supplementation in ovariectomized rats. The levels of femoral total Ca, bone mineral density, and strength were also significantly increased by the FBP diet to levels similar to those of the casein phosphopeptide diet group. [Pg.244]

Micelles in bovine milk contain physiologically significant amounts of calcium and phosphorous because of phosphorylated seryl residues in asl-, aS2- and (3-casein. These casein phosphopeptide (CPP) fragments help to create thermodynamically stable casein micelles super-saturated with calcium and phosphate, thus contributing to the stability of milk during... [Pg.49]

Adamson, N.J. and Reynolds, E.C. 1995. Characterization of tryptic casein phosphopeptides prepared under industrially relevant conditions. Biotechnol. Bioengng. 45, 196-204. [Pg.60]

Hirayama, M., Toyota, K., Hidaka, H., and Naito, H. 1992. Phosphopeptides in rat intestinal digests after ingesting casein phosphopeptides. Biosci. Biotechnol. Biochem. 56, 1128—1129. [Pg.64]

Lee, Y.S., Noguchi, T., and Naito, H. 1983. Intestinal absorption of calcium in rats given diets containing casein or an amino acid mixture the role of casein phosphopeptides. Br. J. Nutr. 49, 67 -76. [Pg.65]

Scholz-Ahrens, K.E. and Schrezenmeir, J. 2000. Effects of bioactive substances in milk on mineral and trace element metabolism with special reference to casein phosphopeptides. Brit. J. Nutr. 84(suppl. 1), 147-153. [Pg.69]

Schuepbach, P., Nesser, J.R., Golliard, M., Rouvet, M., and Guggenheim, B. 1996. Incorporation of casein glycomacropeptides and casein phosphopeptides into the salivary pellicle inhibits adherence of mutans Streptococci. J. Dent. Res. 75, 1779-1788. [Pg.69]

Ellegard, K.H., Gammelgard-Larsen, C., Sorensen, E.S., and Fedosov, S. 1999. Process scale chromatographic isolation, characterization and identification of tryptic bioactive casein phosphopeptides. Int. Dairy J. 9, 639-652. [Pg.254]

Hansen, M., Sandstrom, B., and Lonnerdal, B. 1996. The effect of casein phosphopeptides on zinc and calcium absorption from high phytate infant diets assessed in rat pups and caco-2 cells. Pediatr. Res. 40, 547-552. [Pg.256]

Hansen, M., Sandstrom, B., Jensen, M., and Sorensen, S.S. 1997. Casein phosphopeptides improve zinc and calcium absorption from rice-based but not from whole-grain infant cereal. J. Pediatr. Gastroenterol. Nutr. 24, 56—62. [Pg.256]

Hata, I., Ueda, J., and Otani, H. 1999. Immunostimulatory action of a commercially available casein phosphopeptide preparation, CPP-III, in cell cultures. Milchwissenschaft 54, 3-7. [Pg.257]

Heaney, R.P., Saito, Y., and Orimo, H. 1994. Effect of casein phosphopeptides on absorbability of co-ingested calcium in normal and postmenopausal women. J. Bone Miner. Metab. 12, 77-81. [Pg.257]

Kitts, D.K., Yuan, Y.V., Nagasawa, T., and Moriyama, Y. 1992. Effect of casein, casein phosphopeptide and calcium intake on ileal 45-Ca disappearance and temporal systolic blood pressure in spontaneously hypertensive rats. Br. J. Nutr. 68, 765-781. [Pg.259]

Kopra, N., Scholz-Ahrens, K.-E., and Barth, C. 1992. Effect of casein phosphopeptides on utilization of calcium in vitamin D-replete and vitamin D-deficient rats. Milchwissenschaft 47, 488-493. [Pg.259]

Mellander, O. 1950. The physiological importance of the casein phosphopeptide calcium salts II. Peroral calcium dosage of infants. Acta Soc. Med. Uppsala 55, 247-255. [Pg.263]

Mykkanen, H.M. and Wasserman, R.H. 1980. Enhanced absorption of calcium by casein phosphopeptides in rachitis and normal chicks. J. Nutr. 110, 2141-2148. [Pg.264]

Ono, T., Takagi, Y., and Kunishi, I. 1998. Casein phosphopeptides from casein micelles by successive digestion with pepsin and trypsin. Biosci. Biotechnol. Biochem. 62, 16-21. [Pg.265]

Otani, H., Kihara, Y., and Park, M. 2000. The immunoenhancing property of dietary casein phosphopeptide preparation in mice. Food Agric. Immunol. 12, 165-173. [Pg.266]

Reynolds, E.C. 1998. Anticariogenic complexes of amorphous calcium phosphate stabilized by casein phosphopeptides a review. Spec. Care Dent. 18, 8—16. [Pg.268]

Rose, R.K. 2000a. Binding characteristics of Streptococcus mutans for calcium and casein phosphopeptide. Caries Res. 34, 427-431. [Pg.268]

Rose, R.K. 2000b. Effects of an anticariogenic casein phosphopeptide on calcium diffusion in streptococcal model dental plaques. Arch. Oral Biol. 45, 569-575. [Pg.268]

Saito, Y., Lee, Y.S., and Kimura, S. 1998. Minimum effective dose of casein phosphopeptides (CPP) for enhancement of calcium absorption in growing rats. hit. J. Vitamin. Nutr. Res. 68, 335-340. [Pg.269]

Tsuchita, H., Sekiguchi, I., Kuwata, T., Igarashi, C., and Ezawa, I. 1993. The effect of casein phosphopeptides on calcium utilization in young ovariectomized rats. Z. Emdhrungswiss. 32, 121-130. [Pg.273]

Tsuchita, H., Goto, T., Shimizu, T., Yonehara, Y., and Kuwata, T. 1996. Dietary casein phosphopeptides prevent bone loss in aged ovariectomized rats. J. Nutr. 126, 86-93. [Pg.273]

Yuan, Y.V. and Kitts, D.D. 1991. Confirmation of calcium absorption and femoral utilization in spontaneously hypertensive rats fed casein phosphopeptide supplemented diets. Nutr. Res. 11, 1257-1272. [Pg.276]

Cross, K.J., Huq, N.L., Palamara, J.E., Perich, J.W., and Reynolds, E.C. (2005). Physicochemical characterization of casein phosphopeptide-amorphous calcium phosphate nanocomplexes. J. Biol. Chem. 280, 15362-15369. [Pg.221]

D.J. McCormick, M.W. Holmes, D.C. Muddiman, B.J. Madden, Mapping sites of protein phosphorylation by MS utilizing a chemical-enzymatic approach characterization of products from a-Sl casein phosphopeptides, J. Proteome Res., 4 (2005) 424. [Pg.542]

Augmentation of the Ca reservoir in plaque can also be provided by casein phosphopeptide preparations. Such materials, derived from milk, can bind amorphous CaPi and have been shown to inhibit demineralisation [51] and promote remineralisation [52] of enamel in situ in humans. Rose [53] recently demonstrated that the addition of casein phosphopeptide to a model bacterial plaque in vitro not only provided extra Ca2+-binding sites but also restricted Ca diffusion through the plaque. [Pg.143]

Reynolds EC Remineralization of enamel subsurface lesions by casein phosphopeptide-stabilized calcium phosphate solutions. J Dent Res 1997 76 1587-1595. [Pg.148]

Several different types of dental caries have been described by clinicians. Specifically these are smooth-surface caries, pit and fissure caries, enamel caries, dentinal caries, secondary caries, early childhood caries and root caries [12], All occur by the same essential mechanism, as described above, and all arise as a consequence of a disturbance to the demineralization-remineralization balance. Attack by organic acids produced by bacteria in the plaque favours demineralization, but the natural remineralization processes of the mouth can reverse this. Certain dietary and hygiene behaviours as well as clinical treatments can enhance this natural remineralization provided they occur early enough in the demineralization part of the process. For example, complexes of casein phosphopeptide with amorphous calcium phosphate have been shown in various studies to be capable of enhancing the remineralization step under certain conditions and in specific groups of individuals [16,17]. These are now available commercially as an anticaries treatment for patients. [Pg.4]

Acidic peptides are released in the pH range 5.5-6.2 and phoshorylated peptides are eluted in the pH range 6.9-7.5. Elution of retained peptides can also be performed with sodium phosphate. IMAC has been successfully used for the characterization of casein phosphopeptides in cheese extracts. Phosphoproteins can be separated under very similar conditions as phosphopeptides. IMA sorbents were already used for fractionation of proteins... [Pg.1180]


See other pages where Casein phosphopeptides is mentioned: [Pg.99]    [Pg.82]    [Pg.33]    [Pg.114]    [Pg.89]    [Pg.68]    [Pg.251]    [Pg.351]    [Pg.750]   
See also in sourсe #XX -- [ Pg.114 ]

See also in sourсe #XX -- [ Pg.303 ]




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