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Literature DB >> 19048361

Stability of beta-lactoglobulin A in the presence of sugar osmolytes estimated from their guanidinium chloride-induced transition curves.

Abstract

The stabilizing role of Trehalose, Sucrose, Sorbitol and Mannitol as sugar osmolytes and polyols on beta-lactoglobulin A (beta-lgA) against its chemical denaturation at pH 2.0 and 25 degrees C has been explored by means of UV-vis spectroscopy. It has been observed that DeltaG (D) (o) of beta-lgA in the presence of 10% (w/v) Trehalose, Sucrose, Sorbitol and Mannitol is increased. We report that the functional dependence of DeltaG (D) of proteins in the absence and the presence of sugar osmolytes on denaturant concentration is linear. Trehalose is found to induce remarkable stability of beta-lgA against chemical denaturation. Furthermore, we assumed sugar osmolytes do not affect the secondary and tertiary structures of the native and GdnHCl-denatured states.

Entities: Chemical

Mesh：

Substances：

Year: 2008 PMID： 19048361 DOI： 10.1007/s10930-008-9156-x

Source DB: PubMed Journal: Protein J ISSN： 1572-3887 Impact factor: 2.371

43 in total

1. Second virial coefficients as a measure of protein--osmolyte interactions.

Authors: G T Weatherly; G J Pielak
Journal: Protein Sci Date: 2001-01 Impact factor: 6.725

2. Osmolyte-induced changes in protein conformational equilibria.

Authors: A J Saunders; P R Davis-Searles; D L Allen; G J Pielak; D A Erie
Journal: Biopolymers Date: 2000-04-05 Impact factor: 2.505

Review 3. The osmophobic effect: natural selection of a thermodynamic force in protein folding.

Authors: D W Bolen; I V Baskakov
Journal: J Mol Biol Date: 2001-07-27 Impact factor: 5.469

Review 4. Modulation of globular protein functionality by weakly interacting cosolvents.

Authors: David Julian McClements
Journal: Crit Rev Food Sci Nutr Date: 2002-09 Impact factor: 11.176

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

Authors: A Divsalar; A A Saboury; A A Moosavi-Movahedi; H Mansoori-Torshizi
Journal: Int J Biol Macromol Date: 2006-01-18 Impact factor: 6.953

6. Why is trehalose an exceptional protein stabilizer? An analysis of the thermal stability of proteins in the presence of the compatible osmolyte trehalose.

Authors: Jai K Kaushik; Rajiv Bhat
Journal: J Biol Chem Date: 2003-04-17 Impact factor: 5.157

1. Beneficial effect of sugar osmolytes on the refolding of guanidine hydrochloride-denatured trehalose-6-phosphate hydrolase from Bacillus licheniformis.

Authors: Jiau-Hua Chen; Meng-Chun Chi; Min-Guan Lin; Long-Liu Lin; Tzu-Fan Wang
Journal: Biomed Res Int Date: 2015-01-13 Impact factor: 3.411

1 in total

Stability of beta-lactoglobulin A in the presence of sugar osmolytes estimated from their guanidinium chloride-induced transition curves.

1. Second virial coefficients as a measure of protein--osmolyte interactions.

2. Osmolyte-induced changes in protein conformational equilibria.

Review 3. The osmophobic effect: natural selection of a thermodynamic force in protein folding.

Review 4. Modulation of globular protein functionality by weakly interacting cosolvents.

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

6. Why is trehalose an exceptional protein stabilizer? An analysis of the thermal stability of proteins in the presence of the compatible osmolyte trehalose.

7. The structure of beta-lactoglobulin and its similarity to plasma retinol-binding protein.

8. Increased thermal stability of proteins in the presence of sugars and polyols.

9. Why preferential hydration does not always stabilize the native structure of globular proteins.

10. Protein stabilization and destabilization by guanidinium salts.

1. Beneficial effect of sugar osmolytes on the refolding of guanidine hydrochloride-denatured trehalose-6-phosphate hydrolase from Bacillus licheniformis.