Chapter 13 - Implications of physicochemical properties of proteins in food industry applications

Abstract

The physicochemical properties regulate the functional properties and end-product quality of proteins. The secondary structure of pulse proteins is predominantly constituted of β-sheets, β-strands, and β-turns, while a lower proportion of α-helix. Pulse proteins are a more heat-stable structure and stability is bestowed to the presence of disulphide bonds. Proteins with a greater number of disulphide bonds are considered as heat stable with less susceptibility to proteolysis and act as potential food allergens. Phenolic compounds, thermal processing, irradiation treatment and extraction conditions regulate the solubility of proteins leading to changes in their functionality. The globular proteins possess better functional properties (emulsifying and foaming) due to the presence of nonpolar regions. Tribo-electrostatic separation technique can be used to get protein fractions composed of higher albumin with greater solubility and excellent emulsifying and foaming properties. Enzymatic treatments alter the physicochemical properties leading to a change in their applications. The complex coacervates prepared using various protein-polysaccharide combinations enhance the functionality and applications of proteins. High-pressure treatment, modifies the functionality and digestibility of proteins by altering the structural conformations without causing denaturation. The interest in the use of plant-based proteins particularly from pulses in various food products have increased but also has a drawback of beany flavor as well as lower solubility and digestibility. Efforts have been made to overcome these issues by fermenting using combinations of various bacterial strains. Plant proteins are being studied for their potential in developing meat analogs ingredients that have the ability to develop fibrous structured that imitate real meat in plant protein-based meat analogs.