Auswahl der wissenschaftlichen Literatur zum Thema „Hydrolysats de protéines de pois“
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Zeitschriftenartikel zum Thema "Hydrolysats de protéines de pois"
de Boissieu, D., F. Ammar und C. Dupont. „L'allergie aux hydrolysats de protéines“. Revue Française d'Allergologie et d'Immunologie Clinique 40, Nr. 1 (Januar 2000): 98–104. http://dx.doi.org/10.1016/s0335-7457(00)80031-3.
Der volle Inhalt der QuellePecquet, C., und M. Laurière. „Hydrolysats de protéines du blé : nouveaux allergènes“. Revue Française d'Allergologie et d'Immunologie Clinique 43, Nr. 1 (Januar 2003): 21–23. http://dx.doi.org/10.1016/s0335-7457(02)00010-2.
Der volle Inhalt der QuelleJuchet, A., F. Rancé, A. Broue, F. Bremont und G. Dutau. „Intolérance aux hydrolysats de protéines chez l'enfant“. Revue Française d'Allergologie et d'Immunologie Clinique 33, Nr. 4 (Oktober 1993): 313–14. http://dx.doi.org/10.1016/s0335-7457(05)80052-8.
Der volle Inhalt der QuelleRaheriniaina, Christian E., Z. Randriamahatody, E. Fanjara, E. Fitahia, D. Andrianasolo, H. I. Hantanirina und L. Razanamparany. „Valorisation des sous-produits de la pêche pour l’alimentation des poulets“. Revue d’élevage et de médecine vétérinaire des pays tropicaux 67, Nr. 3 (30.06.2015): 139. http://dx.doi.org/10.19182/remvt.10177.
Der volle Inhalt der QuelleSiala, N., I. Fetni, O. Azzabi, O. Rebah, S. Briki, M. Ben Hariz und A. Maherzi. „Allergie aux hydrolysats de protéines de lait de vache“. Revue Française d'Allergologie 53, Nr. 3 (April 2013): 336. http://dx.doi.org/10.1016/j.reval.2013.02.015.
Der volle Inhalt der Quellede Boissieu, D., und C. Dupont. „Allergie aux hydrolysats de protéines du lait chez l'enfant“. Archives de Pédiatrie 14, Nr. 1 (Januar 2007): 124–26. http://dx.doi.org/10.1016/j.arcped.2006.10.006.
Der volle Inhalt der QuelleIbsaine, O., K. Djenouhat, H. Berrah und Z. Arrada. „P-496 – Allergie aux hydrolysats de protéines chez l'enfant“. Archives de Pédiatrie 22, Nr. 5 (Mai 2015): 359. http://dx.doi.org/10.1016/s0929-693x(15)30672-2.
Der volle Inhalt der QuelleAmmar, F., D. de Boissieu und C. Dupont. „Allergie aux hydrolysats de protéines. À propos de 30 cas“. Archives de Pédiatrie 6, Nr. 8 (August 1999): 837–43. http://dx.doi.org/10.1016/s0929-693x(00)88476-6.
Der volle Inhalt der QuelleLahouel, N., O. Kheroua, F. Mezemaz und D. Saidi. „Évaluation de l’activité antigénique des hydrolysats de protéines du lactosérum camelin“. Revue Française d'Allergologie 56, Nr. 6 (Oktober 2016): 471–76. http://dx.doi.org/10.1016/j.reval.2015.12.001.
Der volle Inhalt der QuelleRIGOURD, V., J. MAGNY, A. AYACHI, M. DUBOIS, C. DECHILLAZ, M. VODOVAR, N. MEDEJEL, D. ANDRIAMANAMIRIJA, C. SLABA und M. VOYER. „Allergie néonatale aux hydrolysats poussés de protéines de lait de vache“. Revue Française d'Allergologie et d'Immunologie Clinique 40, Nr. 2 (März 2000): 185–89. http://dx.doi.org/10.1016/s0335-7457(00)80006-4.
Der volle Inhalt der QuelleDissertationen zum Thema "Hydrolysats de protéines de pois"
Irankunda, Rachel. „Nickel Chelating Peptides & Chromatography : From Peptides Separation Simulation up to their Antioxidant Activities - related Applications“. Electronic Thesis or Diss., Université de Lorraine, 2023. http://www.theses.fr/2023LORR0213.
Der volle Inhalt der QuelleMetal-Chelating Peptides (MCPs), from protein hydrolysates, present various applications in nutrition, pharmacy, cosmetic etc. Yet, the empirical approach generally used to discover bioactive peptides from hydrolysates is time consuming and expensive due to many steps of fractionation, separation and biological activities evaluation. Thus, this PhD aimed to develop a novel approach for MCPs separation prediction using chromatography modelling and simulation based on the analogy between Immobilized Metal ion Affinity Chromatography (IMAC) and Surface Plasmon Resonance (SPR). For the first time, the SPR-IMAC analogy was experimentally investigated on 22 peptides and 70% of them validated this analogy, since peptides well retained in IMAC were also endowed with a good affinity for Ni2+ in SPR. In the second time, peptides with high affinity for Ni2+ (i.e low dissociation constant KD in SPR and a high retention time in IMAC) were used to study the modelling and simulation of peptide concentration profiles at the column outlet in IMAC. Since knowledge of adsorption isotherms was required to perform simulation, it was necessary to develop a methodology for predicting Langmuir isotherm parameters in IMAC from SPR data. The validity of simulation was evaluated by comparing experimental and simulated retention times that should be close for reliable prediction. Therefore, several approaches were evaluated to determine Langmuir sorption parameters, the most interesting one introduces a correction factor on the maximum adsorption capacity qmax alone, assuming that the affinity of peptides for immobilized Ni2+ did not change depending on the technology used (SPR vs. IMAC), thus affinity constant KA was not modified. Meanwhile, industrial application of MCPs and hydrolysates were studied. First, pea protein hydrolysates were produced by either Alcalase® followed by Flavourzyme® (Alc+Flav≤1kDa) or Protamex® followed by Flavourzyme® (Prot+Flav≤1kDa). SwitchSENSE® technology evidences the presence of Ni2+ chelating peptides and antioxidants tests showed that Prot+Flav≤1kDa has higher radical scavenging and reducing power, related to its higher degree of hydrolysis and small-size peptides quantity. Secondly, pea hydrolysates and MCPs were investigated for their ability to inhibit the lipid oxidation in emulsions. They slowed down lipid oxidation through chelation of prooxidant (metals such as Fe2+) reducing primary and secondary oxidation products responsible of deterioration of lipid containing products. Thus, pea hydrolysates and MCPs could be used as antioxidants in food and cosmetic products, as alternative to chemicals such as EDTA, BHT and TBHQ
Le, Coeur Catherine. „Contribution à l'étude d'un hydrolysat pepsique de myoglobine de muscle squelettique rouge de thon Thunnus Albacares : caractérisation des peptides issus de l'hydrolyse étude de l'association hème-peptide“. La Rochelle, 1996. http://www.theses.fr/1996LAROS011.
Der volle Inhalt der QuelleRavallec, Rozenn. „Valorisation d'hydrolysats d'origine marine : optimisation de la concentration en peptides apparentés aux facteurs de croissance et aux agents sécrétagogues : essais in vitro et in vivo“. Brest, 2000. http://www.theses.fr/2000BRES2041.
Der volle Inhalt der QuelleBANIEL, ALAIN. „Etude de la variabilite genotypique et phenotypique de la composition proteique du pois (pisum sativum l. )“. Nantes, 1993. http://www.theses.fr/1993NANT2011.
Der volle Inhalt der QuelleBEN-HDECH, EL-HASSANE. „Texturation d'une farine de pois par cuisson-extrusion : caracterisation microstructurale, ultrastructurale et physico-chimique“. Nantes, 1993. http://www.theses.fr/1993NANT2014.
Der volle Inhalt der QuelleTAMELIKECHT, HINDI FATMA. „Hydrolyse enzymatique de la fraction hydrosoluble des proteines de pois chiche (cicer arietinum) par la bromelaine et l'alpha-chymotrypsine ; caracterisation des hydrolysats et etude de leur immunogenicite“. Paris 5, 1996. http://www.theses.fr/1996PA05N125.
Der volle Inhalt der QuelleChabanon, Gérald. „Hydrolyses enzymatiques d'isolats protéiques issus de tourteaux de colza : cinétique, modélisation, caractérisation et fonctionnalité des peptides“. Vandoeuvre-les-Nancy, INPL, 2005. http://docnum.univ-lorraine.fr/public/INPL/2005_CHABANON_G.pdf.
Der volle Inhalt der QuelleThis thesis made it possible to study obtaining biologically active peptides or with functional properties through the development of processes for the preparation and the hydrolysis of protein isolates resulting from rapeseed cakes. First, a method of preparation of two protein isolates being different by the type of proteins (Globulin or Albumin) was developed. The two isolates do not have good functional properties but their partial hydrolysis by Alcalase 2. 4L improves some of them. Then, the hydrolytic action of commercial proteases (Alcalase 2. 4L, Pronase SG, Neutrase 0. 8L, Prolyve BS, Lypaïne 6500, Orientase 90N, Espérase 7. 5L) on the isolate of globulins was compared. The valorisation of the hydrolysates related to their capacity to promote the growth of animal cells cultivated in a serum-free medium. It was shown that the kinetics of hydrolysis, the size of produced peptides and the biological activity of the hydrolysates are significantly influenced by the specificity of the enzyme and there is a relation enzyme/ degree of hydrolysis (DH)/ targeted activity. Lastly, we showed for three different enzyme/substrate systems (Alcalase / Globulin, Pronase / Globulin and Alcalase / Albumin) that at given DH and pH, the peptide composition of the hydrolysates is independent of the initial enzyme and substrate concentrations and of the temperature. Thus, the prediction of the temporal evolution of the DH, whatever the values of precedent parameters, allows to control the generation of a peptide mixture with targeted properties. A model based on the reaction pathway of Michaelis-Menten was then built in order to simulate the hydrolysis kinetics in batch reactor. For that, limiting phenomena implied in the hydrolysis (inhibition or inactivation of the enzyme, modification of the substrate) were highlighted
Gharsallaoui, Adem. „Microencapsulation séquentielle d'un système lipidique par des biopolymères végétaux (protéines de pois et pectine) : influence des interactions à l'interface huile / eau“. Dijon, 2009. http://www.theses.fr/2009DIJOS053.
Der volle Inhalt der QuelleThe protection and the vectorization of active, food and pharmaceutical molecules, require separating them from their environment by entrapping them in structured matrices able to release them at the precise place and the quite time. When these encapsulation systems are based on dry emulsions, the control of the matrices requires the knowledge of both the properties of the interfacial membranes and those of the drying matrix. The characterization, of the interfacial properties of pea proteins, in presence and absence of pectin, an anionic polyelectrolyte, allows the study of the interactions proteins/pectin at O/W interfaces and their effect on the emulsion stability during spray-drying process. The study of the effect of the properties of the dehydration matrix, maltodextrins, makes it possible to link their interactions with water to the encapsulation efficiency of dry emulsions. The molecular investigation highlights the role of pectin in the stabilization of the secondary structure of pea globulins during drying, which results in a better protection of the encapsulated active molecule. Lastly, the analysis of the release kinetics of a volatile molecule makes it possible to evaluate the barrier properties of the interfacial layers and to identify the release mechanism. The whole of this work at various scales makes it possible to contribute to the understanding of the various mechanisms implied in the emulsion stabilization by multi-layered interfaces containing proteins/polysaccharides, their resistance to spray-drying and finally their capacity to protect fragile compounds
Duval, Frédéric. „Calmodulines et germination chez le pois (Pisum sativum L. ) : aspects biochimiques et moléculaires“. Angers, 2002. http://www.theses.fr/2002ANGE0042.
Der volle Inhalt der QuelleGauvin, Laurence. „Contribution à l'étude de l'extraction des protéines de pois chiche ("Cicer arietinum") en vue d'une application industrielle“. Paris 5, 1994. http://www.theses.fr/1994PA05P057.
Der volle Inhalt der QuelleBücher zum Thema "Hydrolysats de protéines de pois"
Leclerc, Blaise. Je cultive pois, fèves, haricots...: Des protéines dans mon potager ! Terre Vivante Editions, 2013.
Den vollen Inhalt der Quelle findenLeclerc, Blaise. Je cultive pois, fèves, haricots...: Des protéines dans mon potager ! Terre Vivante Editions, 2013.
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