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Dr. J. RAJU
Ph.D. Scholar
Animal Nutrition
PVNR Telangana Veterinary University
THE A1 vs A2 MILK
STORY
Figure from: MILK PROTEIN POLYMORPHISM: DETECTION AND DIFFUSION OF THE GENETIC VARIANTS IN BOS GENUS, Annali della Facoltà
di Medicina Veterinaria, Vol. XIX, 1999. Università degli Studi di Parma ]
Difference in Structure and Digestion of A2 vs. A1
a2 beta casein
Val Tyr Pro Phe Pro Gly Pro Ile Pro Asn Ser Leu Pro
protein chain (209aa)
a1 beta casein Val Tyr Pro Phe Pro Gly Pro Ile His Asn Ser Leu Pro
protein chain (209aa)
A1 releases BCM - 7
Tyr Gly Pro Ile
Reported as strong exorphin Pro Pro
Phe
Adapted from: Gobbetti M, Stepaniak L, De Angelis M, Corsetti A, Di Cagno R. Latent bioactive peptides in milk proteins: proteolytic activation and significance in dairy processing. Crit
Rev Food Sci Nutr. 2002;42(3):223-39. & Jinsmaa, Y & Yoshikawa, M. 1999. Enzymatic release of neocasomorphin and beta-casomorphin from bovine beta-casein. Peptides V20(8), pp
957-962.
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Breed Evolution and Beta Casein type
9
BCM7
• Heart diseases
• Others
13
Recent research on BCM-7
• Previously studies established that:
• Digestion of A1 but not A2 produces protein fragment beta
casomorphin-7 (BCM-7)
• BCM-7 binds opiate receptors and has the potential to interact with
a range of tissues
• Precursor protein A1 is linked to a range of negative health
outcomes
• Recent clinical trials report BCM-7 production to physiologically relevant
levels in the gut of healthy adult humans. (Boutrou et al, 2013)
• A correlation between BCM-7 levels with delayed psychomotor function
in formula fed human infants has been reported (Kost et al, 2009)
• Serum BCM-7 has also been linked to the compromise of breathing in
infants fed A1 containing formula (Wasilewska et al, 2011) .
• A mechanism by which BCM-7 leads to oxidative stress and cell
dysfunction has subsequently been demonstrated (Trivedi et al, 2012).
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Research Highlights