Interaction between dietary bioactive peptides of short length and bile salts in submicellar or micellar state
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- 作者：Justine Guerina ; b ; 1 ; Alexandre Kriznikc ; 1 ; Nick Ramalanjaonad ; Yves Le Rouxa ; b ; Jean-Michel Girardeta ; b ; jean-michel.girardet@univ-lorraine.fr" class="auth_mail" title="E-mail the corresponding author
- 关键词：CMC ; critical micellar concentration ; DLS ; dynamic light scattering ; EMI ; emission fluorescence intensity ; ITC ; isothermal titration calorimetry ; NaC ; sodium cholate ; NaCDC ; sodium chenodeoxycholate ; NaDC ; sodium deoxycholate ; NaGC ; sodium glycocholate ; NaTC ; sodium taurocholate ; NaTCDC ; sodium taurochenodeoxycholate ; NaTDC ; sodium taurodeoxycholate ; pI ; isoelectric point ; TBS ; Tris-buffered saline ; Tris ; trishydroxymethylaminomethane
- 刊名：Food Chemistry
- 出版年：2016
- 出版时间：15 October 2016
- 年：2016
- 卷：209
- 期：Complete
- 页码：114-122
- 全文大小：477 K
文摘
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Fluorescence spectroscopy and DLS were used to highlight peptide-bile salt interaction.
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Antioxidant peptides from milk: LDQW, LQKW and INYW were studied as peptide models.
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Self-aggregated peptides were dissociated by bile salt micelles.
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Released peptides were likely bound to the surface of bile salt micelles.
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INYW could especially interact with bile salts at submicellar concentrations.