Protein/Emulsifier Interactions

Tommy Nylander, Thomas Arnebrant, Marité Cárdenas, Martin Bos, Peter Wilde

Research output: Chapter in Book/Report/Conference proceedingBook chapterResearchpeer-review


An important consequence of protein-lipid interaction is the effect on stability of the protein in solution as well as on its behavior at interfaces. Here we will discuss key aspects of protein aggregation and unfolding as well as the effects of protein structure (random coil proteins versus globular) that are relevant for our understanding protein-lipid interaction. The main types of emulsifiers are the (1) aqueous soluble, surfactant type and (2) lipids with low aqueous solubility. The monomer concentration as defined by cmc is an important parameter for the soluble lipids. For emulsifiers with low aqueous solubility the emulsifier self-assembly structure and its properties control the interaction with proteins. We will therefore summarize the main features of lipid self-assembly. It also allows us to define different plausible scenarios and principles and models for factors that control the interactions in real food (and Pharmaceutical) systems. For the food applications the fate of the lipid during digestion is important and therefore we will discuss some aspects of enzyme-catalyzed lipolysis in terms of the structural evolution. New products and concepts of using protein/emulsifier interactions will be exemplified by illustrating how food nanotechnology possibly can be used for the delivery of functionality.

Original languageEnglish
Title of host publicationFood Emulsifiers and their Applications
Subtitle of host publicationThird Edition
PublisherSpringer International Publishing
Number of pages92
ISBN (Electronic)9783030291877
ISBN (Print)9783030291853
Publication statusPublished - 2019

Subject classification (UKÄ)

  • Chemical Sciences

Free keywords

  • Emulsions
  • Foam
  • Lipid aqueous interface
  • Lipid liquid crystalline phases
  • Lipid self-assembly
  • Polar lipids
  • Protein lipid interactions
  • Protein unfolding


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