Search results for "Pea Proteins"

showing 4 items of 4 documents

Impact of Ageing on Pea Protein Volatile Compounds and Correlation with Odor

2022

Vegetal proteins are of high interest for their many positive aspects, but their ‘beany’ off-flavor is still limiting the consumer’s acceptance. The aim of this work was to investigate the conservation of pea protein isolate (PPI) during time and especially the evolution of their organoleptic quality under two storage conditions. The evolution of the volatile compounds, the odor and the color of a PPI has been investigated during one year of storage. PPI was exposed to two treatments mimicking a lack of control of storage conditions: treatment A with light exposition at ambient temperature (A—Light 20 °C) and treatment B in the dark but with a higher temperature …

pea proteinVolatile Organic CompoundsHot Temperaturestorage conditionsPharmaceutical ScienceHS-SPME-GC-MSOrganic chemistry‘beany’ off-flavorAnalytical Chemistrypea protein; storage conditions; aroma; HS-SPME-GC-MS; ‘beany’ off-flavorQD241-441aromaChemistry (miscellaneous)OdorantsDrug DiscoveryMolecular Medicine[SDV.BV] Life Sciences [q-bio]/Vegetal BiologyPhysical and Theoretical Chemistry[SDV.MP] Life Sciences [q-bio]/Microbiology and ParasitologyPea ProteinsMolecules
researchProduct

Improvement of the techno-functional properties of pea proteins by microfluidization

2017

The use of pea (Pisum sativum (L.)) proteins in the food industry is still limited despite their good environmental sustainability, heath-oriented composition, reliable origin and stable price. However, one of the most important limitations is their low solubility which determines a number of their techno-functional properties. Microfluidization is a non-thermal emerging technology that may modify the structure and the techno-functional properties of pea proteins. Microfluidization combines high shear forces due to the stream speed and direction; impact forces from collisions with the walls and with the fluid itself; and turbulence inside the chamber. The objective of this work was to evalu…

Dynamic high pressureSolubilityPea proteins[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologyTechno-functional propertiesMicrofluidization
researchProduct

Study of the interactions and physicochemical properties of pea and egg white protein mixtures : from the colloidal to the gelled state.

2022

In recent years, due to the growth of world population, people's consumption of animal protein has increased, leading to the increase of greenhouse gas emissions and land occupation. Therefore, it is necessary to partially replace animal protein with vegetable protein to increase the proportion of vegetable protein in daily consumption and developing mixed food systems seems to be one adequate solution. Pea proteins as a source of plant proteins have good nutritional properties but with limited functional properties while egg white (EW) has good functional properties such as gelling and foaming. Thereby, the physicochemical interactions from mixtures of both types of protein needs to be und…

Propriétés thermiquesThermal properties.InteractionFonctionnalitéPea proteinsGelation propertiesPropriétés de gélification[SDE.ES] Environmental Sciences/Environmental and SocietyEgg proteinsFunctionalityProtéines d'oeufProtéines de pois
researchProduct

Influence de l'état protéique sur la dynamique de séparation de phase et de gélification dans un système ternaire aqueux à base de protéines de pois …

2012

Two aqueous systems at 20°C in 0.1 M NaCl and pH 7.2 containing globular pea proteins and sodium alginate were investigated in this study. First, phase behavior of (i) either low-denatured mixed globulins or (ii) their thermally pre-aggregated counterparts - alginate mixtures was compared using a multi-scale approach, by means of phase diagram and microstructure analysis by confocal microscopy. Thermodynamic incompatibility was the main driving force leading to phase separation within the mixtures, which presented according to their initial biopolymer composition both different morphological and time-evolution features of coexisting phases. Thereafter, a cold-set gelation for each system wa…

[SDV.SA] Life Sciences [q-bio]/Agricultural sciencesGelationGlobular pea proteins[ SDV.AEN ] Life Sciences [q-bio]/Food and NutritionAlginatePhase separationNetworkIncompatibilité[ PHYS.COND.CM-GEN ] Physics [physics]/Condensed Matter [cond-mat]/Other [cond-mat.other]RéseauRhéologie[SDV.AEN] Life Sciences [q-bio]/Food and NutritionAggregationProtéines globuliares de poisGélification[CHIM.OTHE] Chemical Sciences/OtherSéparation de phase[ CHIM.OTHE ] Chemical Sciences/OtherAgrégationIncompatibilityRheologyMicrostructure[ SDV.SA ] Life Sciences [q-bio]/Agricultural sciences
researchProduct