Hydrophobicity Enhances the Formation of Protein-Stabilized Foams.

ABSTRACT: Screening proteins for their potential use in foam applications is very laborious and time consuming. It would be beneficial if the foam properties could be predicted based on their molecular properties, but this is currently not possible. For protein-stabilized emulsions, a model was recently introduced to predict the emulsion properties from the protein molecular properties. Since the fundamental mechanisms for foam and emulsion formation are very similar, it is of interest to determine whether the link to molecular properties defined in that model is also applicable to foams. This study aims to link the exposed hydrophobicity with the foam ability and foam stability, using lysozyme variants with altered hydrophobicity, obtained from controlled heat treatment (77 °C for 0-120 min). To es

SUBMITTER: Delahaije RJBM 

PROVIDER: S-EPMC9000900 | biostudies-literature | 2022 Apr

REPOSITORIES: biostudies-literature