Linked Life Data

20411963

Source:http://linkedlifedata.com/resource/pubmed/id/20411963

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
19
pubmed:dateCreated
2010-5-13
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1520-5207
pubmed:author
pubmed:issnType
Electronic
pubmed:day
20
pubmed:volume
114
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6707-12
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Beta-lactoglobulin/folic acid complexes: formation, characterization, and biological implication.
pubmed:affiliation
Institut de recherche sur les nutraceutiques et les aliments fonctionnels (INAF/STELA), Université Laval, Québec, QC, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't