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Short communication: Bovine -casein variants result in different angiotensin I converting enzyme (ACE) inhibitory peptides

C. Weimann^*,1, H. Meisel and G. Erhardt^*

^* Institute of Animal Breeding and Genetics, Ludwigstr. 21B, D-35390 Giessen, Germany
Max Rubner-Institute (MRI), Federal Research Institute of Nutrition and Food, Department of Safety and Quality of Milk and Fish Products, PO Box 6069, D-24121 Kiel, Germany

¹ Corresponding author: Christina.Weimann{at}agrar.uni-giessen.de

Proteins in bovine milk are a common source of bioactive peptides. The peptides are released by the digestion of caseins and whey proteins. Peptides derived from the different genetic variants A, B, C, E, F1, F2, G1, G2, H, I, and J of bovine -casein (CSN3) were investigated for their inhibitory activities against angiotensin I converting enzyme (ACE). Amino acid sequences of the CSN3 variants were analyzed in silico to detect potential ACE inhibitory peptides. Besides known biologically active peptides, exclusive peptides were identified in some CSN3 variants and their biological activity was determined: within CSN3*B and CSN3*C, the ACE inhibitory peptide ASP (IC₅₀ = 242.3; the IC₅₀ value is equivalent to the micromolar concentration of peptide mediating a 50% inhibition of ACE activity) and within CSN3*C the peptide AHHP (IC₅₀ = 847.6) was detected. Furthermore, the peptides VSP (IC₅₀ = 21.8) and ACHP (IC₅₀ = 360.7) were identified in CSN3*F1 and CSN3*G2, respectively.

Key Words: bovine -casein • angiotensin I converting enzyme inhibitory peptide

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