Dilational Viscoelasticity of Proteins Solutions in Dynamic Conditions

Langmuir. 2018 Jun 12;34(23):6678-6686. doi: 10.1021/acs.langmuir.8b00631. Epub 2018 May 31.

Abstract

Drop profile analysis tensiometry used in the oscillating drop mode provides the dilational viscoelasticity of adsorption layers at liquid interfaces. Applied during the progress of adsorption the dynamic surface rheology can be monitored. For β-casein solutions at the same surface pressure values, the larger the dynamic dilational viscoelasticity the longer the adsorption time, i.e., the smaller the studied protein concentration is. For β-lactoglobulin and human serum albumin, the differences in the viscoelasticity values are less or not dependent on the adsorption time at identical surface pressures. The observed effects are caused by the flexibility of BCS, while the globular proteins BLG and HSA do not change their conformation significantly within the adsorption layer.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adsorption
  • Humans
  • Lactoglobulins / chemistry
  • Pressure
  • Proteins / chemistry*
  • Rheology
  • Serum Albumin, Human / chemistry
  • Solutions / chemistry
  • Surface Properties
  • Viscosity
  • Water / chemistry

Substances

  • Lactoglobulins
  • Proteins
  • Solutions
  • Water
  • Serum Albumin, Human