Stability of labile folates is enhanced by binding to milk folate-binding protein

Citation
Ml. Hutchinson et al., Stability of labile folates is enhanced by binding to milk folate-binding protein, AUST J DAIR, 55(2), 2000, pp. 98-98
Citations number
2
Categorie Soggetti
Food Science/Nutrition
Journal title
AUSTRALIAN JOURNAL OF DAIRY TECHNOLOGY
ISSN journal
00049433 → ACNP
Volume
55
Issue
2
Year of publication
2000
Pages
98 - 98
Database
ISI
SICI code
0004-9433(200006)55:2<98:SOLFIE>2.0.ZU;2-N
Abstract
Folic acid is the parent of a number of derivatives that are vitamins, esse ntial for DNA and amino acid synthesis. Almost all naturally occurring fola tes are tetrahydro-folates, which are susceptible to oxidation in air, with loss of vitamin activity. Tetrahydrofolate (H4F) and 10-formyltetrahydrofo late are very labile, 5-methyltetrahydro-folate (5-CH3-H4F) is moderately l abile, while 5-formyltetrahydrofolate is quite stable. The predominant fola te present in milk is 5-CH3-H4F at a concentration of approximately 50 mu g /L. Folate binding protein (FBP) is present in bovine milk at a concentration i n excess of that required to bind all milk folates. The results of this pap er demonstrate that FBP stabilises tetrahydrofolates.