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BACKGROUND There is an increasing trend in the food industry to utilize plant‐based proteins. Pea protein (PP) is one such protein that is a promising alternative emulsifier. However, there is a significant functionality gap between laboratory and commercially produced PP that limits its usage. The physicochemical and emulsification properties of five commercial PP powders were characterized to better understand the functionality gap. RESULTS Four of the five commercial powders displayed low solubility, high surface hydrophobicity, and an abundance of large insoluble aggregates. High‐pressure homogenization was able to break up the aggregates, reduce surface hydrophobicity, and increase solubility. There was a significant correlation between the homogenized solubility and the emulsification properties of the commercial PPs. There was not a significant correlation between the emulsification properties and the other physicochemical properties (unhomogenized solubility, zeta potential, surface hydrophobicity, and interfacial tension). CONCLUSIONS The conformational changes caused by the commercial isolation process may disrupt the correlations between the physicochemical and emulsification properties of PP. Solubility is a key physicochemical property to enable good emulsification properties for PP. Homogenization is an effective step to improve the solubility of commercial PP and therefore promote its functional properties before industrial usage. © 2021 Society of Chemical Industry.

Summary Pea protein is a promising option for plant protein‐based emulsification, but commercial proteins have limited functional properties related to their poor physicochemical properties such as solubility. To address this issue, this research investigated the effects of high‐pressure homogenisation and extraction conditions on the solubility and emulsification properties of pea protein. Heating during extraction can denature pea protein and simulate the reduced functional properties of commercial proteins. Homogenising at 10 000 psi combined with the heating process during extraction significantly improved the solubility and emulsification properties of pea protein. Freeze drying at pH 9.0 improved the solubility of pea protein and lowered the droplet size of resultant emulsions compared to pH 7.0. Extracting the protein in propylene glycol to inhibit hydrophobic interactions slightly improved solubility but decreased the emulsification properties. The combination of homogenisation during heating and freeze drying at an elevated pH produced the optimum solubility and emulsification properties. These results suggest that high‐pressure homogenisation and drying at elevated pH levels can be effective tools to limit the functionality‐reducing effects of denaturation that occurs during the commercial extraction of pea protein. This information can be used to design better production methods for pea protein and improve its functional properties.