Interaction of Tannin with Bovine Serum Albumin by Fluorescence Spectrometry
Kim Dong-Il, Choe Son-Ae, Sin Kye-Ryong
TL;DR
This study investigates how tannin interacts with bovine serum albumin using fluorescence spectrometry, revealing a hydrophobic, stationary state quenching process with a coupling coefficient of one.
Contribution
It provides new insights into the specific hydrophobic interaction mechanism between tannin and BSA through fluorescence analysis.
Findings
Interaction is a stationary state quenching process.
Coupling coefficient is one.
Hydrophobic interaction dominates the binding mechanism.
Abstract
Interaction between tannin and bovine serum albumin (BSA) was examined by the fluorescent quenching. The process of elimination between BSA and tannin was the one of a stationary state, and the coupling coefficient was one. The working strength between the tannin and the beef serum was hydrophobic one.
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Taxonomy
TopicsPhytochemicals and Antioxidant Activities · Plant Gene Expression Analysis · Biochemical and biochemical processes