Добірка наукової літератури з теми "Chromatographie d'affinité sur ions métalliques immobilisés (IMAC)"
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Дисертації з теми "Chromatographie d'affinité sur ions métalliques immobilisés (IMAC)":
Jiang, Kai You. "Etude par chromatographie d'affinité sur ions métalliques immobilisés (IMAC) des relations structure/fonction de l'alpha-chymotrypsine bovine native et glycosylée chimiquement." Compiègne, 1999. http://www.theses.fr/1999COMP1208.
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.
Metal-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
Todorova, Daniela. "Etude par la Chromatographie d'Affinité pour les ions métalliques immobilisés (IMAC) de quelques glycosyl hydrolases natives, recombinantes et de pommes de terre transgéniques." Compiègne, 2001. http://www.theses.fr/2001COMP1362.
Boulis, Yannick. "Étude de la sporamine recombinante exprimée dans le tabac : purification par chromatographie d'affinité pour les ions métalliques immobilisés (IMAC) et caractérisation par spectrométrie de masse en mode électrospray (ESI-MS)." Compiègne, 1998. http://www.theses.fr/1998COMP1183.
Le, Devedec Frantz. "Séparation des oligomères du chitosane par chromatographie d'affinité sur ions métalliques immobilisés." Mémoire, 2008. http://www.archipel.uqam.ca/959/1/M10234.pdf.