Journal
LUMINESCENCE
Volume 31, Issue 3, Pages 782-792Publisher
WILEY
DOI: 10.1002/bio.3024
Keywords
-carotene; astaxanthin; trypsin; pepsin; spectroscopy
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Funding
- National Natural Science Foundation of China [21173071, 21303043]
- Key Research Project of Colleges and Universities of Henan Province [15A150004]
- Doctoral Startup Fund of Xinxiang Medical University [505078]
- Foundation for Fostering of Xinxiang Medical University [2014QN122]
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-Carotene and astaxanthin are two carotenoids with powerful antioxidant properties, but the binding mechanisms of -carotene/astaxanthin to proteases remain unclear. In this study, the interaction of these two carotenoids with trypsin and pepsin was investigated using steady-state and time-resolved fluorescence measurements, synchronous fluorescence spectroscopy, UV-vis absorption spectroscopy and circular dichroism (CD) spectroscopy. The experimental results indicated that the quenching mechanisms of trypsin/pepsin by the two carotenoids are static processes. The binding constants of trypsin and pepsin with these two carotenoids are in the following order: astaxanthin-trypsin>astaxanthin-pepsin>-carotene-trypsin>-carotene-pepsin, respectively. Thermodynamic investigations revealed that the interaction between the two carotenoids and trypsin/pepsin is synergistically driven by enthalpy and entropy, and hydrophobic forces and electrostatic attraction have a significant role in the reactions. In addition, as shown by synchronous fluorescence spectroscopy, UV-vis absorption spectroscopy and CD, the two carotenoids may induce conformational and microenvironmental changes in trypsin/pepsin. The study provides an accurate and full basic data for clarifying the binding mechanisms of the two carotenoids with trypsin/pepsin and is helpful in understanding their effect on protein function and their biological activity in vivo. Copyright (c) 2015 John Wiley & Sons, Ltd.
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