Comparative analysis of refolding of chemically denatured beta-lactoglobulin types A and B using the dilution additive mode |
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Authors: | Divsalar A Saboury A A Moosavi-Movahedi A A Mansoori-Torshizi H |
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Affiliation: | Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran. |
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Abstract: | The kinetic refolding of beta-lactoglobulin (BLG), types A and B, by beta-cyclodextrin, glucose and sorbitol has been investigated in aqueous solution using fluorescence, far UV-CD and UV-spectrophotometric techniques. A new Pd-complex has been used to denature the protein. CD and fluorescence studies indicated that when incubated with sugar, the denatured BLG is refolded into the native-like structure through the dilution additive mode resulting in a higher yield of active protein than without sugar. CD studies show that these sugars can induce a non-native alpha-helical structure in denatured BLG-A and -B, then aid in the refolding of the protein. Based on the present study, these sugars have a different effect on BLG-A than BLG-B because of their differences in protein thermal stability. BLG-A has a higher thermal stability than BLG-B due to differences in the amino acid sequences. |
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