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
Additional Information

Structure view and single mutant data analysis

Study data

No weblogo for data of varying length.
Colors: D E R H K S T N Q A V I L M F Y W C G P
 

Data Distribution

Studies with similar sequences (approximate matches)

Correlation with other assays (exact sequence matches)


Relevant PDB Entries

Structure ID Release Date Resolution Structure Title
4CK4 2013-12-27T00:00:00+0000 1.12 Ovine beta-Lactoglobulin at Atomic Resolution
4NLI 2013-11-14T00:00:00+0000 1.9 Crystal structure of sheep beta-lactoglobulin (space group P3121)
4NLJ 2013-11-14T00:00:00+0000 1.4 Crystal structure of sheep beta-lactoglobulin (space group P1)
6T44 2019-10-12T00:00:00+0000 2.0 Ovine lactoglobulin complex with decanol
4OMW 2014-01-27T00:00:00+0000 2.3 Crystal structure of goat beta-lactoglobulin (orthorhombic form)
4OMX 2014-01-27T00:00:00+0000 2.3 Crystal structure of goat beta-lactoglobulin (trigonal form)
4TLJ 2014-05-30T00:00:00+0000 1.17 Ultra-high resolution crystal structure of caprine Beta-lactoglobulin
4Y0S 2015-02-06T00:00:00+0000 1.9 Goat beta-lactoglobulin complex with pramocaine (GLG-PRM)
7LWC 2021-02-28T00:00:00+0000 3.0 Goat beta-lactoglobulin mutant Q59A
1B0O 1998-11-11T00:00:00+0000 2.5 BOVINE BETA-LACTOGLOBULIN COMPLEXED WITH PALMITATE, LATTICE Z

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
100.0 Beta-lactoglobulin P02754 LACB_BOVIN
98.8 Beta-lactoglobulin P02755 LACB_BUBBU
96.3 Beta-lactoglobulin P02756 LACB_CAPHI
95.7 Beta-lactoglobulin P67976 LACB_SHEEP
95.7 Beta-lactoglobulin P67975 LACB_OVIMU