Electrostatic complexes of whey protein and pectin as foaming and emulsifying agents

Abstract

Five types of electrostatic complex (macromolecular complexes, core-shell particles, and mixed homogeneous particles) were formed between whey protein (whey protein concentrate [WPC]) and pectin. By controlling the thermal treatment, composition, and order of mixing, it was possible to produce complexes that for the same biopolymer concentration gave differing functional properties. All protein-pectin complexes showed higher foaming ability and stability than native or heated WPC without pectin. Native WPC had higher emulsifying ability than protein-pectin complexes but exhibited the lowest emulsion stability. Ingredients based on such ideas might offer the food manufacturer greater control over food structure, stability, and organoleptic properties. ARTICLE HISTORY

Structural and emulsion stabilizing properties of pectin rich extracts obtained from different botanical sources

“…An explanation that can be put forward is the occurrence of pectin-protein interactions during storage due to the high protein content of TP. Most probably, a network will be formed at pH 2.5 by electrostatic interactions between the negatively charge pectin polymers and the positively charged proteins (Oduse, Campbell, Lonchamp, & Euston, 2017). This hypothesis seems plausible when observing the macroscopic picture of the TP pH 2.5 emulsion after 14 days of storage in Figure 6, since this emulsion is the only one with visible phase separation.…”

Food-grade strategies to increase stability of whey protein particles: Particle hardening through aldehyde treatment

“…WPI powder usually contains at least 90% protein material, further complemented with minor fractions of lactose (0.2-2.0 w/w%), fat (0.2-1.5 w/w%), ash (0.3-4.5 w/w%) and moisture (0.2-2.0 w/w%) (Bansal & Bhandari, 2016). In the past couple of years, WPI-based particles have already been produced for encapsulation of bioactive and functional molecules (Bagheri, Madadlou, Yarmand, & Mousavi, 2013;Sung, Xiao, Decker, & McClements, 2015), stabilization of foams and emulsions (Lazidis, et al, 2016;Oduse, et al, 2017) and other food structuring and nutritional purposes (Sağlam, Venema, de Vries, van Aelst, & van der Linden, 2012;Schenkel, Samudrala, & Hinrichs, 2013). However, these particles show a tendency to redissolve in aqueous environment, triggering particle disintegration in water-based systems (Corradini, Demol, Boeve, Ludescher, & Joye, 2017).…”

Complex coacervation between oak protein isolate and gum Arabic: optimization & functional characterization

“…Ratio of protein to polysaccharide, pH, ionic strength, molecular weight, protein charge, polysaccharide charge, temperature, and mechanical parameters such as shear rate, pressure, and time are the factors that affect the complex formation as well as the stability of the formed product. [2,3] Gum Arabic is an important polysaccharide that is widely used in interaction with proteins. The low linear charge density of GA allows it to form complexes with the proteins that are highly charged in nature.…”

“…[4] Polysaccharide molecules such as GA that contain acidic groups are negatively charged over a wide pH range. [3] There have been many studies into the electrostatic interaction of GA with various proteins, including canola protein isolate, [5] soy protein isolate, and gelatin. [6] However, no research has been done so far on the interaction of OPI with any gum.…”