Hydrophobicity, amphilicity, and flexibility: Relation between molecular protein properties and the macroscopic effects of surface activity

Abstract

Their surface activity enables proteins to form and stabilize foam, which can be used for in situ product separation or foam fractionation. Thus, it would be highly desirable to predict the surface activity of proteins based on their molecular properties like hydrophobicity, amphilicity, or structure on primary, secondary, and tertiary level. Ionic strength and pH were adjusted to gain maximum surface activity. The surface activity decreased in the order α lactalbumin > β‑lactoglobulin > trypsinogen > papain. For the theoretical analysis, the database was extended by including 2 hydrophobins into the investigation, since they are known to exhibit an outstanding surface activity. No relation to the macroscopic behavior was found considering the hydrophobicity. I.e., the non-hydrophobins did not differ significantly from each other, and from the hydrophobins, one was significantly hydrophobic, and the other was significantly hydrophilic. Also, no relations were found considering the amphilicity of the secondary structure elements. However, taking into account the tertiary protein structure, it was found that for most of the proteins investigated, the presence of non-buried amphiphilic secondary structure elements in combination with a certain amount of flexibility correlates with the surface activity.

Keywords: Hydrophobic moment; Hydrophobicity; Proteins; Surface activity; pH-dependent charge.