Interactions of milk α- and β-casein with malvidin-3-O-glucoside and their effects on the stability of grape skin anthocyanin extracts
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- 作者：Zhiyong Hea ; zyhe@jiangnan.edu.cn" class="auth_mail" title="E-mail the corresponding author ; Mingzhu Xua ; Maomao Zenga ; Fang Qina ; Jie Chena ; b ; chenjie@jiangnan.edu.cn" class="auth_mail" title="E-mail the corresponding author
- 关键词：Anthocyanin ; Casein ; Interaction ; Fluorescence spectroscopy ; Circular dichroism ; Fourier transform infrared ; Stability
- 刊名：Food Chemistry
- 出版年：2016
- 出版时间：15 May 2016
- 年：2016
- 卷：199
- 期：Complete
- 页码：314-322
- 全文大小：972 K
文摘
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α-, β-casein bound with MG mainly via hydrophilic or hydrophobic interactions.
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α-Casein had a slightly stronger binding affinity toward MG than β-casein.
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MG binding caused different alterations of the secondary structure of α-, β-casein.
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Casein–MG interaction had a positive effect on the stability of GSAE.