| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10542868 | Food Chemistry | 2012 | 7 Pages |
Abstract
⺠Interaction of maltol and bovine serum albumin (BSA) is investigated by multispectroscopic techniques. ⺠Maltol can quench the fluorescence of BSA through a static quenching procedure. ⺠The binding of maltol to BSA is driven mainly by hydrophobic interactions. ⺠Subdomain IIA (Sudlow site I) of BSA is found to be the main binding site for maltol. ⺠The secondary structure of BSA has been changed in the presence of maltol.
Related Topics
Physical Sciences and Engineering
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Authors
Guowen Zhang, Yadi Ma, Lin Wang, Yepeng Zhang, Jia Zhou,