Glycomacropeptide

Glycomacropeptide (GMP) is a glycosolated polypeptide formed during the creation of lactic acid fermented dairy products as a fragment of sweet whey. The unglycosolated form is known as caseinomacropeptide or CMP.

GMP is the third largest fraction of whey protein isolate, after alpha-lactalbumin and beta-lactoglobulin. GMP is formed when the casein micelle that encapsulates milk protein is cleaved by the enzyme chymosin. The 64 terminal polypeptides of Kappa-casein are removed by the enzyme to create GMP.[1]

Unique properties

GMP is unique from other milk peptides in several ways. Kappa-casein is the only glycosolated casein protein and GMP, which makes up much of Kappa-casein, is also glycosolated. The glycans make GMP the only portion of the casein micelle that is water soluble after curdling has occurred, and thus, the only fraction of casein protein to dissolve into the whey.

Additionally, GMP is the only easily attainable source of dietary peptides that does not contain any aromatic amino acids. This makes it a safe source for individuals with phenylketonuria to obtain dietary amino acids, as phenylalanine is an aromatic amino acid.

GMP is also currently being researched for its effects to bind to bacteria through a "decoy effect".[2] GMP contains sialic acid glycans that pathogenic bacteria bind to, competitively reducing the bacteria's ability to bind to epithelial cells.

References

Córdova, Dávalos (March 11, 2019). "Glycomacropeptide Bioactivity and Health: A Review Highlighting Action Mechanisms and Signaling Pathways". Nutrients. 11 (3): 598. doi:10.3390/nu11030598. PMC 6471465. PMID 30870995.
Wolfram, Brück (2006). "The effects of α-lactalbumin and glycomacropeptide on the association of CaCo-2 cells by enteropathogenic Escherichia coli, Salmonella typhimurium and Shigella flexneri". FEMS Microbiology Letters. 259 (1).

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[1] Córdova, Dávalos (March 11, 2019). "Glycomacropeptide Bioactivity and Health: A Review Highlighting Action Mechanisms and Signaling Pathways". Nutrients. 11 (3): 598. doi:10.3390/nu11030598. PMC 6471465. PMID 30870995.

[2] Wolfram, Brück (2006). "The effects of α-lactalbumin and glycomacropeptide on the association of CaCo-2 cells by enteropathogenic Escherichia coli, Salmonella typhimurium and Shigella flexneri". FEMS Microbiology Letters. 259 (1).