Acta Chimica Sinica ›› 2012, Vol. 70 ›› Issue (12): 1379-1384.DOI: 10.6023/A1112156 Previous Articles     Next Articles

Special Topic

日落黄和β-胡萝卜素与牛血清白蛋白相互作用的对比研究

张方圆a,b, 倪永年a,b   

  1. a 南昌大学食品科学与技术国家重点实验室 南昌 330047;
    b 南昌大学化学系 南昌 330031
  • 收稿日期:2011-12-15 修回日期:2012-03-19 出版日期:2012-06-28 发布日期:2012-04-06
  • 通讯作者: 倪永年 E-mail:ynni@ncu.edu.cn
  • 基金资助:

    国家自然科学基金(No. 21065007)和南昌大学食品科学与技术国家重点实验室基金(Nos. SKLFMB-200807, SKLF-TS-200919)资助项目.

A Comparison Study on the Interaction of Sunset Yellow and β-Carotene with Bovine Serum Albumin

Zhang Fangyuana,b, Ni Yongniana,b   

  1. a State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang 330047;
    b Department of Chemistry, Nanchang University, Nanchang 330031
  • Received:2011-12-15 Revised:2012-03-19 Online:2012-06-28 Published:2012-04-06
  • Supported by:

    Project was supported by the National Natural Science Foundation of China (No. 21065007) and the State Key Laboratory of Food Science and Technology of Nanchang University (Nos. SKLFMB-200807, SKLF-TS-200919).

Interaction of Sunset yellow (SY) and β-carotene (BC) with bovine serum albumin (BSA) was investigated under simulated physiological conditions by spectroscopic approaches (fluorescence, UV-Vis, FT-IR and CD). Both SY and BC quenched the intrinsic fluorescence of BSA through static quenching mechanism. The thermodynamic parameters (DH, DS, and DG) obtained from the fluorescence data measured at three different temperatures indicated that the binding of SY to BSA involved electrostatic force, and that of BC to BSA mainly by hydrogen bonding and van der Waals forces. The binding sites number n and binding constants Ka were also obtained. The result of FT-IR spectra and CD showed that the binding of SY to BSA induced conformational changes in BSA.

Key words: β-carotene, Sunset yellow, bovine serum albumin, molecular spectrometry, CD