Aggregation of β‐lactoglobulin and influence of D2O

FEBS Letters

Verheul, Marleen¹  de Kruif, Kees G.¹  Roefs, Sebastianus P.F.M.¹ 

[1] Netherlands Institute for Dairy Research (NIZO), P.O. Box 20, 6710 BA Ede, The Netherlands

关键词: D2O;    β-Lactoglobulin;    Protein stability;    Protein aggregation;    Light scattering;    Differential scanning calorimetry;   

DOI  :  10.1016/S0014-5793(97)01581-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown