The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
β-Lactoglobulin/Folic Acid Complexes: Formation, Characterization, and Biological Implication
Abstract
Beta-lactoglobulin (beta-LG), the major whey protein in bovine milk, binds to a wide range of compounds. Folic acid (FA) is a synthetic form of the B group vitamin known as folates, which are essential cofactors for a variety of physiological processes. The interaction of beta-LG with FA was studied using fluorescence spectroscopy to determine the FA binding constant and mode and the influence of the protein on FA photodegradation. At < or = 20 microM FA, which may be the critical self-association concentration, the binding constant and number are 2.0 (+/-0.6) x 10(6) M(-1) and 1.30 (+/-0.03) when excited at 280 nm and 4.3 (+/-2.2) x 10(5) M(-1) and 1.17 (+/-0.04) at 295 nm, as determined by protein intrinsic fluorescence. FA binds to the surface of beta-LG, possibly in the groove between the alpha-helix and the beta-barrel. Fluorescence analysis of the pterin portion of FA shows that complexation with beta-LG improves FA photostability. It is suggested that beta-LG complexes could be used as an effective carrier of FA in functional foods.
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Citations
Cites
Folic Acid: Nutritional Biochemistry, Molecular Biology, and Role in Disease Processes
Lucock, M. (2000) · Molecular Genetics and Metabolism · doi:10.1006/mgme.2000.3027 · Cited by 815
Chapter 1 Folate‐Mediated One‐Carbon Metabolism
Fox, J. T., & Stover, P. J. (2008) · Vitamins & Hormones · doi:10.1016/s0083-6729(08)00401-9 · Cited by 402
Metadata
- Authors
- Liang, L., & Subirade, M.
- Venue
- The Journal of Physical Chemistry B
- Publisher
- American Chemical Society (ACS)
- Published
- 2010-04-22
- Volume
- 114
- Issue
- 19
- Pages
- 6707-6712
- ISSN
- 1520-5207 (ISSN-L)
- 1520-6106
- OpenAlex
- W2051584011
- Cited by
- 182
- References
- 2
- FWCI
- 3.07
- Type
- journal article
- Language
- en
- Open access
- closed
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