光谱学与光谱分析 |
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Intermolecular Hydrogen Bond between Protein and Flavonoid and Its Contribution to the Stability of the Flavonoids |
FANG Ru, LENG Xiao-jing*, WU Xia, LI Qi, HAO Rui-fang, REN Fa-zheng, JING Hao* |
College of Food Science & Nutritional Engineering, China Agricultural University, Key Laboratory of Functional Dairy Science of Beijing and Ministry of Education, Beijing 100083, China |
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Abstract The interactions between three proteins (BSA, lysozyme and myoglobin) and three flavonoids (quercetin, kaempferol and rutin) were analyzed, using three-dimensional fluorescence spectrometry in combination with UV-Vis spectrometry and Fourier transform infrared (FTIR) spectroscopy. The stabilities of unbound flavonoids and protein-bound flavonoids were compared. The correlation between the interaction and stability was analyzed. The results showed that the hydrophobic interaction was the main binding code in all proteins and flavonoids systems. However, the hydrogen bond has been involved merely in the BSA system. The stability of all three flavonoids (quercetin, kaempferol and rutin) was improved by BSA. There was a great correlation between the hydrogen bonding and the stability of the flavonoids in the presence of BSA. It suggested that the protection of BSA on the flavonoids was due to the intermolecular hydrogen bonding between BSA and flavonoid, and the stronger hydrogen bonding resulted in more protection.
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Received: 2011-03-29
Accepted: 2011-07-18
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Corresponding Authors:
LENG Xiao-jing, JING Hao
E-mail: xiaojing.leng@gmail.com;hao.haojing@gmail.com
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