Molecular Functionality of Plant Proteins from Low- to High-Solid Systems with Ligand and Co-Solute

Int J Mol Sci. 2020 Apr 6;21(7):2550. doi: 10.3390/ijms21072550.

Abstract

In the food industry, proteins are regarded as multifunctional systems whose bioactive hetero-polymeric properties are affected by physicochemical interactions with the surrounding components in formulations. Due to their nutritional value, plant proteins are increasingly considered by the new product developer to provide three-dimensional assemblies of required structure, texture, solubility and interfacial/bulk stability with physical, chemical or enzymatic treatment. This molecular flexibility allows them to form systems for the preservation of fresh food, retention of good nutrition and interaction with a range of microconstituents. While, animal- and milk-based proteins have been widely discussed in the literature, the role of plant proteins in the development of functional foods with enhanced nutritional profile and targeted physiological effects can be further explored. This review aims to look into the molecular functionality of plant proteins in relation to the transport of bioactive ingredients and interaction with other ligands and proteins. In doing so, it will consider preparations from low- to high-solids and the effect of structural transformation via gelation, phase separation and vitrification on protein functionality as a delivery vehicle or heterologous complex. Applications for the design of novel functional foods and nutraceuticals will also be discussed.

Keywords: diffusion; low- to high-solid systems; plant proteins; protein-ligand interactions.

Publication types

  • Review

MeSH terms

  • Algorithms
  • Binding Sites
  • Chemical Phenomena
  • Food Technology
  • Functional Food
  • Kinetics
  • Ligands
  • Models, Molecular
  • Models, Theoretical
  • Molecular Conformation
  • Nutritive Value
  • Plant Proteins / chemistry*
  • Plant Proteins / physiology*
  • Protein Binding
  • Structure-Activity Relationship
  • Temperature
  • Thermodynamics

Substances

  • Ligands
  • Plant Proteins