Comparative analysis of refolding of chemically denatured beta-lactoglobulin types A and B using the dilution additive mode.


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. Study holds ProTherm entries: 20574, 20575, 20576, 20577, 20578, 20579, 20580, 20581, 20582, 20583, 20584, 20585, 20586, 20587, 20588, 20589, 20590, 20591, 20592, 20593, 20594, 20595, 20596, 20597 Extra Details: beta-lactoglobulin; Sugar; Refolding; Thermal stability; alpha-helical structure

Submission Details

ID: JGjQZcMJ4

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:52 p.m.

Version: 1

Publication Details
Divsalar A;Saboury AA;Moosavi-Movahedi AA;Mansoori-Torshizi H,Int. J. Biol. Macromol. (2006) Comparative analysis of refolding of chemically denatured beta-lactoglobulin types A and B using the dilution additive mode. PMID:16417918
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