CAJ | 학술논문

本实验模拟人体生理酸度（ pH 7.4），应用荧光光谱法、紫外光谱法和圆二色光谱法，研究了食品着色剂柠檬黄与牛血清白蛋白（ BSA）的结合性质。结果表明：柠檬黄对BSA内源荧光有较强的猝灭能力，荧光猝灭机制属于形成复合物的单一静态猝灭，计算得出的热力学参数熵变和焓变均为负值，表明氢键和范德华力是驱动柠檬黄-BSA复合物形成的主要作用力，25℃时结合常数已经达到3.04Χ105 L·mol-1，表明柠檬黄与BSA有较强的亲合力。位点竞争实验表明：柠檬黄主要结合至BSA疏水空腔的亚域IIA，即site I位。荧光光谱、紫外光谱和圆二色光谱分析结果显示：柠檬黄与BSA结合引起BSA的表面疏水性增加，α-helix的含量减少，BSA二级结构发生了部分改变。
본실험모의인체생리산도（ pH 7.4），응용형광광보법、자외광보법화원이색광보법，연구료식품착색제저몽황여우혈청백단백（ BSA）적결합성질。결과표명：저몽황대BSA내원형광유교강적졸멸능력，형광졸멸궤제속우형성복합물적단일정태졸멸，계산득출적열역학삼수적변화함변균위부치，표명경건화범덕화력시구동저몽황-BSA복합물형성적주요작용력，25℃시결합상수이경체도3.04Χ105 L·mol-1，표명저몽황여BSA유교강적친합력。위점경쟁실험표명：저몽황주요결합지BSA소수공강적아역IIA，즉site I위。형광광보、자외광보화원이색광보분석결과현시：저몽황여BSA결합인기BSA적표면소수성증가，α-helix적함량감소，BSA이급결구발생료부분개변。
The binding characteristics between tartrazine and bovine serum albumin( BSA)were investigated by fluorescence,UV-vis absorption and circular dichroism( CD)spectroscopy under simulative physiological conditions (pH 7. 4). The results showed that tartrazine had a strong ability to quench the intrinsic fluorescence of BSA,the fluorescence quenching was a single static quenching process. Thermodynamic analysis of the binding data obtained at different temperatures showed that the binding process was primarily driven by hydrogen bonds and van der Waals forces. The binding constant at 298K was calculated to be 3. 04Χ105 L·mol-1 ,indicating that a high affinity exis-ted between tartrazine and BSA. The site marKers competitive experiments suggested that tartrazine and warfarin shared a common binding site corresponding to the subdomain IIA( site I)of BSA. Analysis of synchronous fluores-cence,UV-vis absorption and CD spectra demonstrated that the addition of tartrazine resulted in the conformational alteration of BSA with a decreasing in α-helix structure. The determination of protein surface hydrophobicity( PSH) indicated that tartrazine binding to BSA caused an increasing in the PSH.