β-Lactoglobulin as nanotransporter - Part II: Characterization of the covalent protein modification by allicin and diallyl disulfide
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- 作者：Sandra Catharina Wildea ; 1 ; swilde@foodtech.uni-kiel.de" class="auth_mail" title="E-mail the corresponding author ; Christian Treitzb ; 1 ; c.treitz@iem.uni-kiel.de" class="auth_mail" title="E-mail the corresponding author ; Julia Katharina Kepplera ; Tomas Koudelkab ; Kalpana Palania ; Andreas Tholeyb ; Harshadrai M. Rawelc ; Karin Schwarza
- 关键词：Beta-lactoglobulin ; Covalent modification ; LC&ndash ; MS ; CD ; DLS ; Thiol ; Allicin ; Garlic ; Diallyl disulfide
- 刊名：Food Chemistry
- 出版年：2016
- 出版时间：15 April 2016
- 年：2016
- 卷：197
- 期：part_PA
- 页码：1022-1029
- 全文大小：1071 K
文摘
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Allicin and diallyl disulfide were covalently bound by β-lactoglobulin.
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The free thiol group of (Cys121) was modified to S-allylmercaptocysteine.
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Binding of allicin did not influence enzymatic digestion.
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Binding of allicin induced a moderate loosening of protein folding.
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Binding of allicin did not induce dissociation of β-lactoglobulin dimers.