Protein stabilizing potential of simulated honey sugar cocktail under various denaturation conditions |
| |
Authors: | Yin-How Wong Saad Tayyab |
| |
Affiliation: | Biomolecular Research Group, Biochemistry Programme, Institute of Biological Sciences, Faculty of Science, University of Malaya, 50603 Kuala Lumpur, Malaysia |
| |
Abstract: | Protein stabilizing potential of simulated honey sugar cocktail (SHSC) against chemical and thermal denaturations was studied using bovine serum albumin (BSA) as the model protein. The two-step, three-state transition of urea denaturation of BSA became a single-step, two-state transition along with the shift in the whole transition curve towards higher urea concentrations in the presence of increasing SHSC concentrations [8–20% (w/v)] as revealed by far-UV CD, fluorescence and UV difference spectroscopic results. Far-UV and near-UV CD spectra, UV difference spectra, ANS fluorescence and three-dimensional fluorescence results suggested significant retention of native-like conformation in 4.6 M urea-denatured BSA in the presence of 20% (w/v) SHSC. A significant shift was also noticed in thermal and GdnHCl denaturation curves of BSA in the presence of 20% (w/v) SHSC. Taken together, all these results suggested significant stabilization of BSA against urea, GdnHCl and thermal denaturations by SHSC. |
| |
Keywords: | |
本文献已被 ScienceDirect 等数据库收录! |
|