title: Tailoring structure and technological properties of plant proteins using high hydrostatic pressure.
abstract: The demand for proteins is rising and alternatives to meat proteins are necessary since animal husbandry is expensive and intensive to the environment. Plant proteins appear as an alternative; however, their techno-functional properties need improvement. High-pressure processing (HPP) is a non-thermal technology that has several applications including the modification of proteins. The application of pressure allows modifying proteins' structure hence allowing to change several of their properties, such as hydration, hydrophobicity, and hydrophilicity. These properties may influence the solubility of proteins and their ability to stabilize emulsions or foams, create aggregates or gels, and their general role in stability and texture of food commodities. Commonly HPP decreases the proteins' solubility yet increasing their surface hydrophobicity exposing sulfhydryl groups, which promotes aggregation or gelation or enhance their ability to stabilize emulsions/foams. However, these effects are not verifiable for all the proteins and are immensely dependent on the type and concentration of the protein, environmental conditions (pH, ionic strength, and co-solutes), and HPP conditions. This review collects and critically discusses the available information on how HPP affects the structure of plant proteins and how their techno-functional properties can be tailored using this approach.
authors.affiliation: a QOPNA - Organic Chemistry, Natural and Agro-Food Products Research Unit, Department of Chemistry , University of Aveiro , Aveiro , Portugal.
authors.forename: Rui P
authors.identifier: http://orcid.org/0000-0002-9112-5276
authors.initials: RP
authors.lastname: Queirós
authors.affiliation: a QOPNA - Organic Chemistry, Natural and Agro-Food Products Research Unit, Department of Chemistry , University of Aveiro , Aveiro , Portugal.
authors.forename: Jorge A
authors.identifier: http://orcid.org/0000-0002-5536-6056
authors.initials: JA
authors.lastname: Saraiva
authors.affiliation: a QOPNA - Organic Chemistry, Natural and Agro-Food Products Research Unit, Department of Chemistry , University of Aveiro , Aveiro , Portugal.
authors.forename: José A Lopes
authors.identifier: http://orcid.org/0000-0002-2863-1790
authors.initials: JAL
authors.lastname: da Silva
mesh_terms: D000818:Animals; D004044:Dietary Proteins / Q000737:chemistry*; D004655:Emulsions / Q000737:chemistry; D005511:Food Handling; D005524:Food Technology; D005782:Gels / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D057927:Hydrophobic and Hydrophilic Interactions; D006874:Hydrostatic Pressure; D008460:Meat; D015394:Molecular Structure; D009994:Osmolar Concentration; D010940:Plant Proteins / Q000737:chemistry*; D012995:Solubility; D013696:Temperature
chemical_list: D004044:Dietary Proteins; D004655:Emulsions; D005782:Gels; D010940:Plant Proteins
keywords: Protein's structure; aggregation; emulsifying activity; gelation; solubility; surface hydrophobicity