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Stability of β-Lactoglobulin A in the Presence of Sugar Osmolytes Estimated from Their Guanidinium Chloride-Induced Transition Curves

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Abstract

The stabilizing role of Trehalose, Sucrose, Sorbitol and Mannitol as sugar osmolytes and polyols on beta-lactoglobulin A (β-lgA) against its chemical denaturation at pH 2.0 and 25 °C has been explored by means of UV–vis spectroscopy. It has been observed that ΔG oD of β-lgA in the presence of 10% (w/v) Trehalose, Sucrose, Sorbitol and Mannitol is increased. We report that the functional dependence of ΔG 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 β-lgA against chemical denaturation. Furthermore, we assumed sugar osmolytes do not affect the secondary and tertiary structures of the native and GdnHCl-denatured states.

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Abbreviations

β-lgA:

β-Lactoglobulin A

ε:

Molar absorption coefficient

Δε292 :

Difference molar absorbance at 292 nm

ΔG D :

Gibbs free energy change

ΔG oD :

Gibbs free energy change in absence of denaturant at 25 °C

GdnHCl:

Guanidinium chloride

y N :

Optical property of the native state

y D :

Optical property of the denatured state

C m :

Midpoint of chemical denaturation

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Acknowledgments

The financial supports of Islamic Azad University, Science and Research Branch and Omidieh Branch are gratefully acknowledged.

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Authors and Affiliations

  1. Department of Chemistry, Science and Research Branch, Islamic Azad University, Tehran, Iran

    Zohreh Saadati

  2. Department of Chemistry, Omidieh Branch, Islamic Azad University, Khuzestan, Iran

    Zohreh Saadati

  3. Department of Chemistry, Laboratory of Biophysical Chemistry, University of Isfahan, Isfahan, 81746-73441, Iran

    Abdol-Khalegh Bordbar

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  1. Zohreh Saadati
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  2. Abdol-Khalegh Bordbar
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Correspondence to Abdol-Khalegh Bordbar.

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Saadati, Z., Bordbar, AK. Stability of β-Lactoglobulin A in the Presence of Sugar Osmolytes Estimated from Their Guanidinium Chloride-Induced Transition Curves. Protein J 27, 455–460 (2008). https://doi.org/10.1007/s10930-008-9156-x

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  • DOI: https://doi.org/10.1007/s10930-008-9156-x

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