Publicação
Unravelling the influence of novel food processing technologies in the functional and organoleptic properties of alternative protein sources
| Resumo: | Plant-derived proteins have been emerging and growing in interest due to their attractive technological functional properties and the trend to replace animal-derived proteins. Pea protein (PP) has attracted significant interest of the food industry and scientific community due to its nutritional and biological value, and recognized low allergenicity. Moreover, its commercial availability coupled with the previous attributes, make of this protein a good option for utilization in a broad range of food applications. However, one of the biggest challenges of using such commercially available PP ingredients lies on their frequently limited solubility, often aggravated by their high level of processing before going to the market, hampering the design of functional ingredients. This work’s main goal is to disclose the potential of two distinct processing technologies: ohmic heating (OH) and high pressure processing (HPP), as innovative and sustainable protein modification techniques for improving the solubility and functionality of a commercial PP. The application of OH and HPP (alone or combined with temperature (HPP + T)) to improve protein solubility was investigated. Generally, OH application and HPP + T application resulted in enhanced solubility. The structural characterization of the proteins suggested the transformation of insoluble macroaggregates/precipitates into soluble aggregates. Moreover, OH application, at higher treatment temperatures, may have induced protein hydrolytic cleavage of the peptide bond to some extent. The potential of OH and HPP to improve the functional properties of commercial PP was further explored. OH and HPP + T application (particularly at the highest pressure/temperature combination), resulted in an increase of the foaming capacity and foam stability of PP dispersions. The gels obtained by cold-set gelation of PP dispersions treated by OH and HPP, displayed distinctive rheological properties from those obtained from the untreated PP. Due the observed potential of OH to modify PP, its capacity to induce the formation of amyloid fibrils (as interesting protein structures holding potential to improve a variety of functional properties) in egg white protein (EWP) and PP dispersions (as potential substitute for eggless formulations) was also explored. It was shown that OH can be used as an alternative to conventional heating to induce the formation of amyloid-like fibrils in EWP dispersions. Despite the impact of OH on PP fibrillation being limited, under the conditions studied, OH promoted PP fibrillation to some extent or resulted in rearrangement of the existing fibrils. This work confirmed the potential of both processing technologies to be used as effective tools for tailoring PP functionality aiming at developing innovative protein systems. It also provided strong indications of the beneficial impact of OH and HPP to improve the texture/mouthfeel of PP ingredients. |
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| Autores principais: | Avelar, Zita Sofia Barbosa |
| Assunto: | Commercial pea protein Emerging processing technologies Protein functionality Protein modification Solubility Funcionalidade proteica Modificação proteica Proteína de ervilha comercial Solubilidade Tecnologias emergentes de processamento Ciências Agrárias::Biotecnologia Agrária e Alimentar |
| Ano: | 2024 |
| País: | Portugal |
| Tipo de documento: | tese de doutoramento |
| Tipo de acesso: | acesso aberto |
| Instituição associada: | Universidade do Minho |
| Idioma: | inglês |
| Origem: | RepositóriUM - Universidade do Minho |
| Resumo: | Plant-derived proteins have been emerging and growing in interest due to their attractive technological functional properties and the trend to replace animal-derived proteins. Pea protein (PP) has attracted significant interest of the food industry and scientific community due to its nutritional and biological value, and recognized low allergenicity. Moreover, its commercial availability coupled with the previous attributes, make of this protein a good option for utilization in a broad range of food applications. However, one of the biggest challenges of using such commercially available PP ingredients lies on their frequently limited solubility, often aggravated by their high level of processing before going to the market, hampering the design of functional ingredients. This work’s main goal is to disclose the potential of two distinct processing technologies: ohmic heating (OH) and high pressure processing (HPP), as innovative and sustainable protein modification techniques for improving the solubility and functionality of a commercial PP. The application of OH and HPP (alone or combined with temperature (HPP + T)) to improve protein solubility was investigated. Generally, OH application and HPP + T application resulted in enhanced solubility. The structural characterization of the proteins suggested the transformation of insoluble macroaggregates/precipitates into soluble aggregates. Moreover, OH application, at higher treatment temperatures, may have induced protein hydrolytic cleavage of the peptide bond to some extent. The potential of OH and HPP to improve the functional properties of commercial PP was further explored. OH and HPP + T application (particularly at the highest pressure/temperature combination), resulted in an increase of the foaming capacity and foam stability of PP dispersions. The gels obtained by cold-set gelation of PP dispersions treated by OH and HPP, displayed distinctive rheological properties from those obtained from the untreated PP. Due the observed potential of OH to modify PP, its capacity to induce the formation of amyloid fibrils (as interesting protein structures holding potential to improve a variety of functional properties) in egg white protein (EWP) and PP dispersions (as potential substitute for eggless formulations) was also explored. It was shown that OH can be used as an alternative to conventional heating to induce the formation of amyloid-like fibrils in EWP dispersions. Despite the impact of OH on PP fibrillation being limited, under the conditions studied, OH promoted PP fibrillation to some extent or resulted in rearrangement of the existing fibrils. This work confirmed the potential of both processing technologies to be used as effective tools for tailoring PP functionality aiming at developing innovative protein systems. It also provided strong indications of the beneficial impact of OH and HPP to improve the texture/mouthfeel of PP ingredients. |
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