Casein-Derived Peptide, Casein Glycomacropeptide, Casein Glycopeptide, Casein Macropeptide, Caseinoglycomacropeptide, Caséinoglycomacropeptide, Glicomacropéptido, Glycomacropeptide de Caséine, Glycomacropeptide de Kappa-Caséine, Glycopeptide de Caséine, Kappa-Casein Glycomacropeptide, Macropeptide de Caséine, Peptide Dérivé de Caséine.
Glycomacropeptide is a type of short protein. It is formed from a milk protein during the process of making cheese. Unlike most other proteins, glycomacropeptide contains very little of the amino acid phenylalanine.
People take glycomacropeptide for heart disease, preventing dental cavities, gout, infant development, liver disease, phenylketonuria, mental conditions, and weight loss.
How does work?
Glycomacropeptide might help improve weight loss by increasing the release of chemicals that make people feel full. Glycomacropeptide might also attach to certain bacteria, viruses, and toxins and prevent them from infecting people.
Insufficient Evidence to Rate Effectiveness for...
- Phenylketonuria. Early research suggests that replacing a typical phenylalanine-free diet with foods enriched in glycomacropeptide maintains blood levels of the amino acid phenylalanine and does not negatively affect health and kidney function in people with phenylketonuria. But compared to a typical phenylalanine-free diet, people with phenylketonuria prefer to eat foods enriched in glycomacropeptide.
- Weight loss. Clinical research suggests that replacing one or two meals daily with a meal-replacement supplement containing glycomacropeptide for one year while also following an energy restricted diet reduces weight by approximately 24 lbs compared to baseline. However, the effect of the glycomacropeptide supplement does not appear to be different than taking a similar skim milk powder supplement.
- Heart disease.
- Dental cavities.
- Gout.
- Infant development.
- Liver disease.
- Mental conditions.
- Other conditions.
SLIDESHOW
Vitamin D Deficiency: How Much Vitamin D Is Enough? See SlideshowGlycomacropeptide is POSSIBLY SAFE when taken by mouth as a food supplement for up to one year.
Pregnancy and breast-feeding: Not enough is known about the use of glycomacropeptide during pregnancy and breast-feeding. Stay on the safe side and avoid use.Children: Glycomacropeptide is POSSIBLY SAFE when added to formula and given to infants. However, there is some concern that formula containing glycomacropeptide might increase the risk of blood threonine levels becoming too high (hyperthreoninemia).
The appropriate dose of glycomacropeptide depends on several factors such as the user's age, health, and several other conditions. At this time there is not enough scientific information to determine an appropriate range of doses for glycomacropeptide. Keep in mind that natural products are not always necessarily safe and dosages can be important. Be sure to follow relevant directions on product labels and consult your pharmacist or physician or other healthcare professional before using.
Natural Medicines Comprehensive Database rates effectiveness based on scientific evidence according to the following scale: Effective, Likely Effective, Possibly Effective, Possibly Ineffective, Likely Ineffective, and Insufficient Evidence to Rate (detailed description of each of the ratings).
Report Problems to the Food and Drug Administration
You are encouraged to report negative side effects of prescription drugs to the FDA. Visit the FDA MedWatch website or call 1-800-FDA-1088.
Andersson Y, Hammarstrom ML, Lonnerdal B, et al. Formula feeding skews immune cell composition toward adaptive immunity compared to breastfeeding. J Immunol 2009;183(7):4322-4328. View abstract.
Bruck WM, Kelleher SL, Gibson GR, Graverholt G, Lonnerdal BL. The effects of alpha-lactalbumin and glycomacropeptide on the association of CaCo-2 cells by enteropathogenic Escherichia coli, Salmonella typhimurium and Shigella flexneri. FEMS Microbiol Lett 2006;259(1):158-162. View abstract.
Burton-Freeman, B. M. Glycomacropeptide (GMP) is not critical to whey-induced satiety, but may have a unique role in energy intake regulation through cholecystokinin (CCK). Physiol Behav 2008;93(1-2):379-387. View abstract.
Chernikov MP, Stan EI, Vasilevskaia LS, Shlygin GK. [Heterogeneity of the kappa-casein glycomacropeptide and physiological activity of its fractions]. Vopr Pitan 1979;(5):22-26. View abstract.
Chlygin GK, Vasilevskaia LS, Chernikov MP, Nikol'skaia GV. [Anti-gastrin effect of glycomacropeptide]. Biull Eksp Biol Med 1971;72(12):9-13. View abstract.
Daddaoua A, Puerta V, Zarzuelo A, et al. Bovine glycomacropeptide is anti-inflammatory in rats with hapten-induced colitis. J Nutr 2005;135(5):1164-1170. View abstract.
Dalbeth N, Gracey E, Pool B, et al. Identification of dairy fractions with anti-inflammatory properties in models of acute gout. Ann Rheum Dis 2010;69(4):766-769. View abstract.
Janer C, Diaz J, Pelaez C, Requena T. The Effect of Caseinomacropeptide and Whey Protein Concentrate on Streptococcus mutans adhesion to polystyrene surfaces and cell aggregation. J Food Quality 2007;27(3):233-238.
Janer C, Diaz J, Pelaez C, Requena T. The Effect of Caseinomacropeptide and Whey Protein Concentrate on Streptococcus mutans adhesion to polystyrene surfaces and cell aggregation. J Food Quality 2007;27(3):233-238. View abstract.
Kawasaki Y, Isoda H, Shinmoto H, et al. Inhibition by kappa-casein glycomacropeptide and lactoferrin of influenza virus hemagglutination. Biosci Biotechnol Biochem 1993;57(7):1214-1215. View abstract.
Kawasaki Y, Isoda H, Tanimoto M, et al. Inhibition by lactoferrin and kappa-casein glycomacropeptide of binding of Cholera toxin to its receptor. Biosci Biotechnol Biochem 1992;56(2):195-198. View abstract.
Keogh, J. B. and Clifton, P. The effect of meal replacements high in glycomacropeptide on weight loss and markers of cardiovascular disease risk. Am J Clin Nutr 2008;87(6):1602-1605. View abstract.
Keogh, J. B., Woonton, B. W., Taylor, C. M., Janakievski, F., Desilva, K., and Clifton, P. M. Effect of glycomacropeptide fractions on cholecystokinin and food intake. Br J Nutr 2010;104(2):286-290. View abstract.
Li EW, Mine Y. Immunoenhancing effects of bovine glycomacropeptide and its derivatives on the proliferative response and phagocytic activities of human macrophagelike cells, U937. J Agric Food Chem 2004;52(9):2704-2708. View abstract.
Li EW, Mine Y. Technical note: Comparison of chromatographic profile of glycomacropeptide from cheese whey isolated using different methods. J Dairy Sci 2004;87(1):174-177. View abstract.
Lim K, van Calcar SC, Nelson KL, Gleason ST, Ney DM. Acceptable low-phenylalanine foods and beverages can be made with glycomacropeptide from cheese whey for individuals with PKU. Mol Genet Metab 2007;92(1-2):176-178. View abstract.
Mikkelsen TL, Bakman S, Sorensen ES, Barkholt V, Frokiaer H. Sialic acid-containing milk proteins show differential immunomodulatory activities independent of sialic acid. J Agric Food Chem 2005;53(20):7673-7680. View abstract.
Mikkelsen TL, Rasmussen E, Olsen A, Barkholt V, Frokiaer H. Immunogenicity of kappa-casein and glycomacropeptide. J Dairy Sci 2006;89(3):824-830. View abstract.
Nakajima K, Tamura N, Kobayashi-Hattori K, et al. Prevention of intestinal infection by glycomacropeptide. Biosci Biotechnol Biochem 2005;69(12):2294-2301. View abstract.
Nakano T, Silva-Hernandez ER, Ikawa N, Ozimek L. Purification of kappa-casien glycomacropeptide from sweet whey with undetectable level of phenylalanine. Biotechnol Prog 2002;18(2):409-412. View abstract.
Ney DM, Hull AK, van Calcar SC, Liu X, Etzel MR. Dietary glycomacropeptide supports growth and reduces the concentrations of phenylalanine in plasma and brain in a murine model of phenylketonuria. J Nutr 2008;138(2):316-322. View abstract.
Ney, D. M., Gleason, S. T., van Calcar, S. C., MacLeod, E. L., Nelson, K. L., Etzel, M. R., Rice, G. M., and Wolff, J. A. Nutritional management of PKU with glycomacropeptide from cheese whey. J Inherit Metab Dis 2009;32(1):32-39. View abstract.
Quero J, Carcia P, Vento M, et al. Reduction of hyperthreoninemia in term infants fed a whey predominant formula without Glycomacropeptide. J Pediatric Gastroenterology and Nutrition 1997;24(4):491.
Requena P, Daddaoua A, Guadix E, et al. Bovine glycomacropeptide induces cytokine production in human monocytes through the stimulation of the MAPK and the NF-kappaB signal transduction pathways. Br J Pharmacol 2009;157(7):1232-1240. View abstract.
Requena P, Daddaoua A, Martinez-Plata E, et al. Bovine glycomacropeptide ameliorates experimental rat ileitis by mechanisms involving downregulation of interleukin 17. Br J Pharmacol 2008;154(4):825-832. View abstract.
Requena P, Gonzalez R, Lopez-Posadas R, et al. The intestinal antiinflammatory agent glycomacropeptide has immunomodulatory actions on rat splenocytes. Biochem Pharmacol 2010;79(12):1797-1804. View abstract.
Rigo J, Boehm G, Georgi G, et al. An infant formula free of glycomacropeptide prevents hyperthreoninemia in formula-fed preterm infants. J Pediatr Gastroenterol Nutr 2001;32(2):127-130. View abstract.
Rutherfurd KJ, Gill HS. Peptides affecting coagulation. Br J Nutr 2000;84 Suppl 1:S99-102. View abstract.
Sandstrom O, Lonnerdal B, Graverholt G, Hernell O. Effects of alpha-lactalbumin-enriched formula containing different concentrations of glycomacropeptide on infant nutrition. Am J Clin Nutr 2008;87(4):921-928. View abstract.
Stan EI, Chernikov MP. [Physiological activity of kappa-casein glycomacropeptide]. Vopr Med Khim 1979;25(3):348-352. View abstract.
Stan EI, Groisman SD, Krasil'shchikov KB, Chernikov MP. [Effect of kappa-casein glycomacropeptide on gastrointestinal motility in dogs]. Biull Eksp Biol Med 1983;96(7):10-12. View abstract.
Tanimoto M, Kawasaki Y, Dosako S, Ahiko K, Nakajima I. Large-scale preparation of k-casein glycomacropeptide from rennet casein whey. Biosci Biotech Biochem 1992;56(1):140-141.
van Calcar SC, MacLeod EL, Gleason ST, et al. Improved nutritional management of phenylketonuria by using a diet containing glycomacropeptide compared with amino acids. Am J Clin Nutr 2009;89(4):1068-1077. View abstract.
Varsanovich EA, Usacheva NT, Stan EI, Vasil'ev AV, Chernikov MP. [Chemical composition of casein glycomacropeptide components]. Vopr Med Khim 1976;22(5):648-652. View abstract.
Vasilevskaia LS, Stan EI, Chernikov MP, Shlygin GK. [Inhibiting action of glycomacropeptide on stomach secretion induced by various humoral stimulants]. Vopr Pitan 1977;(4):21-24. View abstract.
Veldhorst MA, Nieuwenhuizen AG, Hochstenbach-Waelen A, et al. A breakfast with alpha-lactalbumin, gelatin, or gelatin + TRP lowers energy intake at lunch compared with a breakfast with casein, soy, whey, or whey-GMP. Clin Nutr 2009;28(2):147-155. View abstract.
Veldhorst MAB, Nieuwenhuizen AG, Hochstenbach-Waelen A, et al. Effects of high or normal casein-, soy-, or whey with or without GMP- protein breakfasts on satiety, 'satiety' hormones, and plasma amino acid responses. Appetite 2007;49(1):336.
Veldhorst, M. A., Nieuwenhuizen, A. G., Hochstenbach-Waelen, A., Westerterp, K. R., Engelen, M. P., Brummer, R. J., Deutz, N. E., and Westerterp-Plantenga, M. S. Effects of complete whey-protein breakfasts versus whey without GMP-breakfasts on energy intake and satiety. Appetite 2009;52(2):388-395. View abstract.
Wang B, Yu B, Karim M, et al. Dietary sialic acid supplementation improves learning and memory in piglets. Am J Clin Nutr 2007;85(2):561-569. View abstract.