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Relevance of the Functional Properties of Enzymatic Plant Protein Hydrolysates in Food Systems

Wouters, Arno G.B., Rombouts, Ine, Fierens, Ellen, Brijs, Kristof, Delcour, Jan A.
Comprehensive reviews in food science and food safety 2016 v.15 no.4 pp. 786-800
egg albumen, emulsifying properties, environmental impact, enzymatic hydrolysis, foaming, food processing, foods, gelation, hydrophobicity, molecular weight, plant proteins, production costs, protein hydrolysates, protein sources, sensory properties, solubility, structure-activity relationships, texture
Proteins play a crucial role in determining texture and structure of many food products. Although some animal proteins (such as egg white) have excellent functional and organoleptic properties, unfortunately, they entail a higher production cost and environmental impact than plant proteins. It is rather unfortunate that plant protein functionality is often insufficient because of low solubility in aqueous media. Enzymatic hydrolysis strongly increases solubility of proteins and alters their functional properties. The latter is attributed to 3 major structural changes: a decrease in average molecular mass, a higher availability of hydrophobic regions, and the liberation of ionizable groups. We here review current knowledge on solubility, water‐ and fat‐holding capacity, gelation, foaming, and emulsifying properties of plant protein hydrolysates and discuss how these properties are affected by controlled enzymatic hydrolysis. In many cases, research in this field has been limited to fairly simple set‐ups where functionality has been assessed in model systems. To evolve toward a more widely applied industrial use of plant protein hydrolysates, a more thorough understanding of functional properties is required. The structure–function relationship of protein hydrolysates needs to be studied in depth. Finally, test model systems closer to real food processing conditions, and thus to real foods, would be helpful to evaluate whether plant protein hydrolysates could be a viable alternative for other functional protein sources.