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  • 标题:Binding properties of β-lactoglobulin with polyphenols – A review
  • 本地全文:下载
  • 作者:Ana – Maria OANCEA ; Nicoleta STĂNCIUC ; Gabriela RÂPEANU
  • 期刊名称:Annals of the University Dunarea de Jos of Galati. Fascicle VI : Food Technology
  • 印刷版ISSN:1843-5157
  • 电子版ISSN:2068-259X
  • 出版年度:2016
  • 卷号:40
  • 期号:2
  • 页码:9-19
  • 出版社:Galati University Press
  • 摘要:Bovine β-lactoglobulin is the most abundant whey protein secreted in the milk ofmost mammals but not in the human, rodents and lagomorphs milk. The biologicalfunction of this protein is still not completely understood, but it is believed to berelated to its globular structure and the presence of an internal cavity called calyxor β-barrel, where small hydrophobic molecules can bind. Recent studies revealedthat β-lactoglobulin has at least three binding sites, located in the internal core ofthe calyx, at the dimer interface and in the hydrophobic region between α-helixand β-barrel. In particular, this review focuses on the studies presenting β–lactoglobulin as potential carrier for polyphenolic compounds, molecules wellknownfor their beneficial health effects. Regarding the polyphenols binding site,several studies indicated that it is located outside the protein calyx.
  • 关键词:bovine β–lactoglobulin; binding affinity; Tanford transition;polyphenols
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