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https://hdl.handle.net/1822/89363
Registo completo
Campo DC | Valor | Idioma |
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dc.contributor.author | Avelar, Zita Sofia Barbosa | por |
dc.contributor.author | Saraiva, Jorge A. | por |
dc.contributor.author | Vicente, A. A. | por |
dc.contributor.author | Rodrigues, Rui Miguel Martins | por |
dc.date.accessioned | 2024-03-07T19:52:39Z | - |
dc.date.issued | 2024 | - |
dc.identifier.citation | Avelar, Z., Saraiva, J. A., Vicente, A. A., & Rodrigues, R. M. (2024, May). Unravelling the impact of ohmic heating on commercial pea protein structure. Food Hydrocolloids. Elsevier BV. http://doi.org/10.1016/j.foodhyd.2024.109748 | por |
dc.identifier.issn | 0268-005X | por |
dc.identifier.uri | https://hdl.handle.net/1822/89363 | - |
dc.description.abstract | Pea protein (PP) has attracted the attention of the food industry and the scientific community as a substitute for more established plant proteins such as soy proteins. However, commercial PP often displays poor solubility which limits its functionality and further use by the food industry. To overcome this challenging issue, plant protein modification techniques for improved functionality have been investigated. Ohmic heating (OH) is an emergent thermo-electrical processing technology which has demonstrated potential in modifying protein structure and therefore its functionality. In this work, the potential use of OH has a physical technique for protein modification was investigated. Therefore, a commercial PP was submitted to OH application, at treatment temperatures ranging from 90 to 150 °C and the potential changes in PP solubility upon OH application were evaluated. An increase in protein solubility of ca. 240 % was observed after OH application at 150 °C. Protein structural characterization was performed, suggesting PP structural rearrangement, rather than unfolding, upon OH application. Furthermore, OH application presumably promoted the dissociation of the insoluble aggregates already present in the commercial PP sample. Moreover, higher treatment temperatures (particularly from 110 °C onwards) may have induced protein hydrolytic cleavage of the peptide bond to some extent, leading to the formation of mainly small soluble aggregates and peptide fragments. These results open novel perspectives for the use of OH as a promising tool for improving commercial PP solubility and, therefore, enabling its tailored application in the food industry. | por |
dc.description.sponsorship | This study was supported by the Portuguese Foundation for Science and Technology (FCT) under the scope of the strategic funding of UIDB/04469/2020 unit, and by LABBELS–Associate Laboratory in Biotechnology, Bioengineering and Microelectromechanical Systems, LA/P/0029/2020. This work also received financial support through the projects UIDB/50006/2020 and UIDP/50006/2020, funded by FCT/MCTES through national funds to LAQV-REQUIMTE. Zita Avelar acknowledges the Foundation for Science and Technology (FCT) for its fellowship SFRH/BD/146347/2019. | por |
dc.language.iso | eng | por |
dc.publisher | Elsevier 1 | por |
dc.relation | info:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDB%2F04469%2F2020/PT | por |
dc.relation | info:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDB%2F50006%2F2020/PT | por |
dc.relation | info:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDP%2F50006%2F2020/PT | por |
dc.relation | info:eu-repo/grantAgreement/FCT/OE/SFRH%2FBD%2F146347%2F2019/PT | por |
dc.rights | restrictedAccess | por |
dc.subject | Commercial pea protein | por |
dc.subject | Emergent processing technology | por |
dc.subject | Physical modification | por |
dc.subject | Solubility | por |
dc.subject | Structural characterization | por |
dc.title | Unravelling the impact of ohmic heating on commercial pea protein structure | por |
dc.type | article | eng |
dc.peerreviewed | yes | por |
dc.relation.publisherversion | https://www.sciencedirect.com/science/article/pii/S0268005X24000225 | por |
oaire.citationVolume | 150 | por |
dc.identifier.eissn | 1873-7137 | por |
dc.identifier.doi | 10.1016/j.foodhyd.2024.109748 | por |
dc.date.embargo | 10000-01-01 | - |
sdum.journal | Food Hydrocolloids | por |
Aparece nas coleções: | CEB - Publicações em Revistas/Séries Internacionais / Publications in International Journals/Series |
Ficheiros deste registo:
Ficheiro | Descrição | Tamanho | Formato | |
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1-s2.0-S0268005X24000225-main.pdf Acesso restrito! | 3,08 MB | Adobe PDF | Ver/Abrir |