| |
|
|
| Registros recuperados : 1 | |
| 1. |  | WU, A.; PROCHNIK, S.; JENKINS, J.; SALSE, J.; HELLSTEN, U.; MURAT, F.; PERRIER, X.; RUIZ, M.; SCALABRIN, S.; TEROL, J.; TAKITA, M. A.; LABADIE, K.; POULAIN, J.; COULOUX, A.; JABBARI, K.; CATTONARO, F.; DEL FABBRO, C.; PINOSIO, S.; ZUCCOLO, A.; CHAPMAN, J.; GRIMWOOD, J.; TADEO, F. O R.; ESTORNELL, L. H.; MUÑOZ-SANZ, J. V.; IBANEZ, V.; HERRERO-ORTEGA, A.; ALEZA, P.; PÉREZ-PÉREZ, J.; RAMÓN, D.; BRUNEL, D.; LUROM, F.; CHEN, C.; FARMERIE, W. G.; DESANY, B.; KODIRA, C.; MOHIUDDIN, M.; HARKINS, T.; FREDRIKSON, K.; BURNS, P.; LOMSADZE, A.; BORODOVSKY, M.; REFORGIATO, G.; ASTUA, J. de F.; QUETIER, F.; NAVARRO, L.; ROOSE, M.; WINCKER, P.; SCHMUTZ, J.; MORGANTE, M.; MARCOS ANTONIO MACHADO; MANUEL TALON. Sequencing of diverse mandarin, pummelo and orange genomes reveals complex history of admixture during citrus domestication. Nature biotechnology, n. 7,v. 32, July, 2014.| Biblioteca(s): Embrapa Mandioca e Fruticultura. |
|    |
| Registros recuperados : 1 | |
|
|
|
 | Acesso ao texto completo restrito à biblioteca da Embrapa Agroindústria de Alimentos. Para informações adicionais entre em contato com ctaa.biblioteca@embrapa.br. |
Registro Completo
|
Biblioteca(s): |
Embrapa Agroindústria de Alimentos. |
|
Data corrente: |
31/12/2023 |
|
Data da última atualização: |
17/01/2024 |
|
Tipo da produção científica: |
Artigo em Periódico Indexado |
|
Circulação/Nível: |
A - 2 |
|
Autoria: |
LANDIM, A. P. M.; TIBURSKI, J. H.; SILVA, C. M.; JULIANO, P.; ROSENTHAL, A. |
|
Afiliação: |
ANA PAULA MIGUEL LANDIM, UFRRJ; JULIA HAUCK TIBURSKI, UFRRJ; CAROLINE MELLINGER SILVA, CTAA; PABLO JULIANO, CSIRO Agriculture and Food; AMAURI ROSENTHAL, CTAA. |
|
Título: |
Potential Application of High Hydrostatic Pressure on the Production of Hydrolyzed Proteins with Antioxidant and Antihypertensive Properties and Low Allergenicity: A Review. |
|
Ano de publicação: |
2023 |
|
Fonte/Imprenta: |
Foods, v. 12, n. 630, 2023. |
|
DOI: |
https://doi.org/10.3390/foods12030630 |
|
Idioma: |
Inglês |
|
Conteúdo: |
The high hydrostatic pressure (HHP) process has been studied for several applications in food technology and has been commercially implemented in several countries, mainly for non-thermal pasteurization and shelf-life extension of food products. HHP processing has been demonstrated to accelerate proteolytic hydrolysis at a specific combination of pressure and pressure-holding time for a given protein source and enzyme. The enzymatic hydrolysis of proteins is a well-known alternative to producing biologically active peptides, with antioxidant and antihypertensive capacity, from different food protein sources. However, some of these protein sources contain allergenic epitopes which are often not degraded by traditional hydrolysis. Moreover, the peptide profile and related biological activity of a hydrolysate depend on the protein source, the enzymes used, the parameters of the proteolysis process (pH, temperature, time of hydrolysis), and the use of other technologies such as HHP. The present review aims to provide an update on the use of HHP for improving enzymatic hydrolysis, with a particular focus on studies which evaluated hydrolysate antihypertensive and antioxidant capacity, as well as residual allergenicity. Overall, HHP has been shown to improve the biological properties of hydrolysates. While protein allergenicity can be reduced with traditional hydrolysis, HHP can further reduce the allergenicity. Compared with traditional hydrolysis methods, HHP-assisted protein hydrolysis offers a greater opportunity to add value to protein-rich products through conversion into high-end hydrolysate products with enhanced nutritional and functional properties. MenosThe high hydrostatic pressure (HHP) process has been studied for several applications in food technology and has been commercially implemented in several countries, mainly for non-thermal pasteurization and shelf-life extension of food products. HHP processing has been demonstrated to accelerate proteolytic hydrolysis at a specific combination of pressure and pressure-holding time for a given protein source and enzyme. The enzymatic hydrolysis of proteins is a well-known alternative to producing biologically active peptides, with antioxidant and antihypertensive capacity, from different food protein sources. However, some of these protein sources contain allergenic epitopes which are often not degraded by traditional hydrolysis. Moreover, the peptide profile and related biological activity of a hydrolysate depend on the protein source, the enzymes used, the parameters of the proteolysis process (pH, temperature, time of hydrolysis), and the use of other technologies such as HHP. The present review aims to provide an update on the use of HHP for improving enzymatic hydrolysis, with a particular focus on studies which evaluated hydrolysate antihypertensive and antioxidant capacity, as well as residual allergenicity. Overall, HHP has been shown to improve the biological properties of hydrolysates. While protein allergenicity can be reduced with traditional hydrolysis, HHP can further reduce the allergenicity. Compared with traditional hydrolysis methods, HHP-assisted protein hy... Mostrar Tudo |
|
Palavras-Chave: |
Antihypertensive activity; Antioxidant capacit; High hydrostatic pressure. |
|
Thesagro: |
Tecnologia de Alimento. |
|
Thesaurus NAL: |
Allergenicity; Antioxidants; Enzymatic hydrolysis; Food technology; Pressure. |
|
Categoria do assunto: |
Q Alimentos e Nutrição Humana |
|
Marc: |
LEADER 02621naa a2200289 a 4500
001 2160371
005 2024-01-17
008 2023 bl uuuu u00u1 u #d
024 7 $ahttps://doi.org/10.3390/foods12030630$2DOI
100 1 $aLANDIM, A. P. M.
245 $aPotential Application of High Hydrostatic Pressure on the Production of Hydrolyzed Proteins with Antioxidant and Antihypertensive Properties and Low Allergenicity$bA Review.$h[electronic resource]
260 $c2023
520 $aThe high hydrostatic pressure (HHP) process has been studied for several applications in food technology and has been commercially implemented in several countries, mainly for non-thermal pasteurization and shelf-life extension of food products. HHP processing has been demonstrated to accelerate proteolytic hydrolysis at a specific combination of pressure and pressure-holding time for a given protein source and enzyme. The enzymatic hydrolysis of proteins is a well-known alternative to producing biologically active peptides, with antioxidant and antihypertensive capacity, from different food protein sources. However, some of these protein sources contain allergenic epitopes which are often not degraded by traditional hydrolysis. Moreover, the peptide profile and related biological activity of a hydrolysate depend on the protein source, the enzymes used, the parameters of the proteolysis process (pH, temperature, time of hydrolysis), and the use of other technologies such as HHP. The present review aims to provide an update on the use of HHP for improving enzymatic hydrolysis, with a particular focus on studies which evaluated hydrolysate antihypertensive and antioxidant capacity, as well as residual allergenicity. Overall, HHP has been shown to improve the biological properties of hydrolysates. While protein allergenicity can be reduced with traditional hydrolysis, HHP can further reduce the allergenicity. Compared with traditional hydrolysis methods, HHP-assisted protein hydrolysis offers a greater opportunity to add value to protein-rich products through conversion into high-end hydrolysate products with enhanced nutritional and functional properties.
650 $aAllergenicity
650 $aAntioxidants
650 $aEnzymatic hydrolysis
650 $aFood technology
650 $aPressure
650 $aTecnologia de Alimento
653 $aAntihypertensive activity
653 $aAntioxidant capacit
653 $aHigh hydrostatic pressure
700 1 $aTIBURSKI, J. H.
700 1 $aSILVA, C. M.
700 1 $aJULIANO, P.
700 1 $aROSENTHAL, A.
773 $tFoods$gv. 12, n. 630, 2023.
Download
Esconder MarcMostrar Marc Completo |
|
Registro original: |
Embrapa Agroindústria de Alimentos (CTAA) |
|
|
Biblioteca |
ID |
Origem |
Tipo/Formato |
Classificação |
Cutter |
Registro |
Volume |
Status |
Fechar
|
| Nenhum registro encontrado para a expressão de busca informada. |
|
|
