Pectin-Plant protein systems and their application

The techno-functional properties of plant protein are often inferior to those of animal origin, mainly due to denaturation during extraction. They require improvement for easier incorporation into food products, and combinations with pectin were tested for this purpose. Coacervates, formed mainly by electrostatic interactions, and conjugates, formed by covalent binding, improved protein solubility around the isoelectric point, surface activity and emulsion and foam stability. Active (often hydrophobic) ingredients were encapsulated by conjugates or bilayers or within nanoparticles to stabilise them in a hydrophilic environment and to control their release. Coacervates were also able to mask the bitter taste of plant proteins by blocking electrostatic interactions with taste receptors, and fibrous compounds were prepared as meat replacers.. Pectins were well suitable for many combinations with plant proteins in food systems owing to their variety of properties resulting from botanical origin or modification. The impact of pectin structure on the different interactions, however, has been studied only to a limited extent, and not all results were convincing. Additional work, using well defined and characterised pectin samples, is required for a better understanding of the interactions, aimed at an extended plant protein application for human nutrition.

Automated summary

Plant proteins often have lower techno-functional properties compared to animal proteins due to denaturation during extraction. Combining plant proteins with pectin can improve solubility and stability. Pectin's variety of properties make it suitable for combinations with plant proteins in food systems.