Vitamin B 12 and its binding proteins in milk from cow and buffalo in relation to bioavailability of B 12

Sergey N. Fedosov*, Ebba Nexo, Christian W. Heegaard

*Corresponding author af dette arbejde

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review


Milk is an important source of highly bioavailable vitamin B 12 (cobalamin) in human nutrition. In most animal products, vitamin B 12 is strongly bound to various specific protein carriers. The 2 vitamin B 12 -specific proteins, predominantly transcobalamin (TC) and haptocorrin (HC), were earlier found in milk from Holstein Friesian cows and in human or sow milk, respectively. As the type of vitamin B 12 binders may influence bioavailability of the vitamin, we examined vitamin B 12 carriers in pooled milk specimens derived from European and Indian cow and buffalo herds. The total endogenous vitamin B 12 was comparable in all milk pools (≈3 nM), but the vitamin-carriers varied considerably: TC + caseins in Danish cows, TC + HC in Indian cows and buffaloes, and mainly HC in Italian buffaloes. Danish cow milk contained half as much TC as vitamin B 12 , and the surplus vitamin was all attached via a single coordination bond to abundantly available histidine residues of casein. The specific binding proteins in Indian cow milk (TC + HC) approximately matched the molar content of vitamin B 12 . Milk from the 2 buffalo breeds contained more specific binders than vitamin B 12 , and the surplus proteins included the unsaturated TC ≈ 3 nM (Indian stock), or both TC ≈ 4 nM and HC ≈ 23 nM (Italian stock). The abundant HC of the latter sample bound nearly all endogenous vitamin B 12 . We tested (in vitro) the transfer of vitamin B 12 from milk proteins to human carriers, involved in the intestinal uptake. The bovine TC-vitamin B 12 complex rapidly dissociated at pH 2 (τ 1/2 < 1 min, 37°C) and was susceptible to digestion with trypsin + chymotrypsin (pH 7.5). Transfer of vitamin B 12 from the precipitated bovine casein (pH 2) to human carriers proceeded with τ 1/2 ≈ 7 min (37°C) and τ 1/2 ≈ 35 min (20°C). Liberation of vitamin B 12 from buffalo HC was hampered because of its pH stability and slow proteolysis. Nutritional availability of vitamin B 12 is expected to be high in cow milk (with TC-vitamin B 12 and casein-vitamin B 12 complexes) but potentially constrained in buffalo milk (with HC-vitamin B 12 ). This especially concerns the Italian buffalo milk, where a high excess of HC was found. We speculate whether the isolated stock of Italian buffalo maintained the ancestral secretion of carriers (HC ≫ vitamin B 12 , TC ≈ 0), whereas intensive crossbreeding of cows and buffaloes from other regions caused a change to TC ≤ vitamin B 12 , with low or absent HC. The substitution of HC by less sturdy carriers is apparently more beneficial to human consumers as far as vitamin B 12 bioavailability is concerned.

TidsskriftJournal of Dairy Science
Sider (fra-til)4891-4905
Antal sider15
StatusUdgivet - jun. 2019


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