Aggregation of β‐lactoglobulin and influence of D2O

Aggregation of β‐lactoglobulin and influence of D2O

The conformational stability of β‐lactoglobulin increases in D2O over that in H2O. This is concluded from an increase in peak temperature by about 3°C of differential scanning calorimetry (DSC) thermograms and from a decrease in overall aggregation rate. However, effects of pH and salt concentration...

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Veröffentlicht in:FEBS letters 1998-01, Vol.421 (3), p.273-276
Hauptverfasser: Verheul, Marleen, Roefs, Sebastianus P.F.M., de Kruif, Kees G.
Format: Artikel
Sprache:eng
Schlagworte:
Calorimetry, Differential Scanning
D2O
Deuterium Oxide
Differential scanning calorimetry
Hydrogen-Ion Concentration
Kinetics
Lactoglobulins - chemistry
Light scattering
Protein aggregation
Protein stability
Sodium Chloride
Water
β-Lactoglobulin
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Zusammenfassung:The conformational stability of β‐lactoglobulin increases in D2O over that in H2O. This is concluded from an increase in peak temperature by about 3°C of differential scanning calorimetry (DSC) thermograms and from a decrease in overall aggregation rate. However, effects of pH and salt concentration on the heat‐induced aggregation (reaction kinetics, DSC thermograms and aggregate growth) are similar in H2O and D2O. This indicates that the mechanism of heat‐induced aggregation of β‐lactoglobulin is not significantly affected by replacement of H2O with D2O.
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(97)01581-0