المؤلفون: Chapeau, Anne Laure

مرشدي الرسالة: Rennes, Agrocampus Ouest, Bouhallab, Saïd

مصطلحات موضوعية: Coacervation hétéroprotéique, Protéines sériques, Bioactif, Encapsulation, Heteroprotein coacervation, Whey protein, Bioactive, Vitamin

الوصف: Les aliments fonctionnels connaissent aujourd’hui un intérêt grandissant. Pour leur formulation, l'encapsulation de bioactifs représente une voie intéressante et les protéines de lactosérum (PS) présentent de bonnes potentialités en tant qu'agents d’encapsulation. Des travaux antérieurs ont démontré que deux PS, la beta-lactoglobuline (BLG) et la lactoferrine (LF), peuvent former spontanément des co-assemblages par coacervation complexe, une technologie d'encapsulation connue. Cette thèse étudie la coacervation BLG-LF pour l'encapsulation d'un bioactif modèle, la vitamine B9. En testant une gamme de pH et de ratios molaires, les conditions optimales de coacervation B9-PS sont obtenues dans l'eau, à pH 5,5, avec un ratio molaire LF:B9:BLG de 1:5:10, permettant d’atteindre des rendements de coacervation de 45 à 55%, et d’encapsulation de B9 de 98 %.L’échelle de production des coacervats est augmentée avec succès du µL au L, avec des solutions protéiques de qualité commerciale et un mélangeur statique. Les rendements de coacervation et d’encapsulation sont conservés, avec l’encapsulation d’environ 4 mg de B9/g coacervats. Par ailleurs, les coacervats montrent un effet protecteur de la forme native de B9 vis-à-vis des UV, de l’oxydation et pendant la lyophilisation. Une étude in vivo chez le rat démontre une augmentation de la biodisponibilité de B9 lorsque administrée sous forme de coacervats. Les coacervats apparaissent stables lorsqu’ils sont resuspendus en gouttelettes dans du lait. Ce travail permet d’approfondir les connaissances sur la coacervation hétéroprotéique et s
Encapsulation of bioactives is relevant for the development of functional foods. Food proteins as encapsulating agents could match the objective of industries to develop “clean label” products. Moreover, whey proteins (WP) exhibit good potentialities as encapsulating agents. Previous works have demonstrated that the WPs, beta-lactoglobulin (BLG) and lactoferrin (LF), are able to spontaneously co-assemble by complex coacervation. This study explores the ability of BLG-LF coacervates as a potential carrier for the encapsulation of a model bioactive, vitamin B9. Throughout screening experiments, we determined the domains where B9-WP coacervation occured according to a tested range of pH, proteins and vitamin concentrations and molar ratios. Optimal conditions for coacervation were found in water, at pH 5.5, with LF:B9:BLG molar ratio of 1:5:10, affording coacervation yields of 45 to 55% and B9 encapsulation up to 98%.Coacervation was scaled-up from laboratory to bench scale using commercial-grade protein sources and static mixing. Final efficiencies were obtained with coacervates containing 4 mg of B9/g coacervates. Under degradative conditions (UV light irradiation, oxidation, freeze-drying), WP coacervates provided good protective properties limiting chemical degradation of native B9. In vivo oral administration of B9-WP coacervates in rats enhanced the plasmatic concentrations of B9 compared to unencapsulated B9. In addition, good physical stability over time was found after incorporated and resuspension of formed coacervates in milk. The combined results of this thesis p

الإتاحة: http://www.theses.fr/2017NSARB300/documentTest

المؤلفون: Chapeau, Anne Laure, Hamon, Pascaline, Bouhallab, Said, Bertrand, N., Poncelet, D.

المساهمون: Science et Technologie du Lait et de l'Oeuf (STLO), Institut National de la Recherche Agronomique (INRA)-AGROCAMPUS OUEST, Faculty of Pharmacy, CHU de Quebec Research Center, Université Laval Québec (ULaval), Laboratoire de génie des procédés - environnement - agroalimentaire (GEPEA), Institut Universitaire de Technologie - Nantes (IUT Nantes), Université de Nantes (UN)-Université de Nantes (UN)-Université de Nantes - UFR des Sciences et des Techniques (UN UFR ST), Université de Nantes (UN)-Université de Nantes (UN)-Institut Universitaire de Technologie Saint-Nazaire (IUT Saint-Nazaire), Université de Nantes (UN)-Ecole Polytechnique de l'Université de Nantes (EPUN), Université de Nantes (UN)-École nationale vétérinaire, agroalimentaire et de l'alimentation Nantes-Atlantique (ONIRIS)-Centre National de la Recherche Scientifique (CNRS)-Université Bretagne Loire (UBL)-IMT Atlantique (IMT Atlantique), Institut Mines-Télécom Paris (IMT)-Institut Mines-Télécom Paris (IMT)-Institut Universitaire de Technologie - La Roche-sur-Yon (IUT La Roche-sur-Yon), Université de Nantes (UN)

المصدر: 25. International Conference on Bioencapsulation
https://hal.science/hal-01512156Test
25. International Conference on Bioencapsulation, Jul 2017, La Chapelle sur Erdre, France
http://bioencapsulation.net/2017_La_ChapelleTest/

مصطلحات موضوعية: nutrients, whey protein, coacervarion, polymère, stabilité, nature conservation, bioavailability, encapsulation, conservation, vitamine, solubilité, substance nutritive, stabilité physicochimique, industrie agro-alimentaire, biodisponibilité, protéine de lactosérum, coacervation, [SDV.AEN]Life Sciences [q-bio]/Food and Nutrition, [SDV.IDA]Life Sciences [q-bio]/Food engineering

جغرافية الموضوع: La Chapelle sur Erdre, France

الوصف: INTRODUCTION AND OBJECTIVESWhile functional foods have prompted growing interest to enhance the daily intakes of specific nutrients and to prevent deficiencies , their processes and storage can affect stability, solubility and bioavailability. To overcome these limitations, one alternative is the encapsulation of agents acting into carriers. To ensure industrial sustainability, such encapsulating material should be natural food-grade components (biocarriers), using economical and reliable raw materials and processes. The complex coacervation consists in mixing two polymers of opposite charges. Coacervation exploits the balance of electrostatic interactions between the two biopolymers to form a supramolecular assembly. Coacervation may display high shell integrity and encapsulation efficiency, good controlledrelease properties and mild preparation conditions. Thesefeatures are interesting to reduce the industrial processing costs (Yan & Zhang, 2014). Whey proteins (WP) is by- products of the dairy industry, providing intrinsic biological properties. Two specific whey proteins has been selected β-lactoglobulin (BLG) and Lactoferrin (LF) as they able to co-assemble by complex coacervation. Recently the proof of concept that LF-BLG complex coacervates efficiently entrap vitamin B9 (B9) hasbeen established at laboratory scale (Chapeau et al., 2016). This work focuses on the scale-up production of B9-WP coacervates for potential industrial applications. Coacervation is known to be highly sensitive to processing i.e. working volume, interfaces, and mixing conditions. Empirical scale-up could therefore result in increased costs, resources and efforts (Lemetter et al., 2004). Moreover, B9-WP coacervates shouldpreserve the bioavailability of B9 during oral delivery. As a result, this study aims at: 1) investigating the scale-up production of B9-WP coacervate by comparing two mixing systems (in batch or in continuous), and 2) exploring the bioavailability of orally administered B9-WP coacervates.

العلاقة: hal-01512156; https://hal.science/hal-01512156Test; https://hal.science/hal-01512156/documentTest; https://hal.science/hal-01512156/file/20170327_Abstract-BRG_Nantes2017%281%29_%7B9C63F006-E801-43C9-A590-91E7E411FCAC%7D.pdfTest; PRODINRA: 389663

الإتاحة: https://hal.science/hal-01512156Test
https://hal.science/hal-01512156/documentTest
https://hal.science/hal-01512156/file/20170327_Abstract-BRG_Nantes2017%281%29_%7B9C63F006-E801-43C9-A590-91E7E411FCAC%7D.pdfTest

المؤلفون: Chapeau, Anne Laure, Hamon, Pascaline, Rousseau, Florence, Croguennec, Thomas, Poncelet, Denis, Bouhallab, Said

المساهمون: Science et Technologie du Lait et de l'Oeuf (STLO), Institut National de la Recherche Agronomique (INRA)-AGROCAMPUS OUEST, Laboratoire de génie des procédés - environnement - agroalimentaire (GEPEA), Institut Universitaire de Technologie - Nantes (IUT Nantes), Université de Nantes (UN)-Université de Nantes (UN)-Université de Nantes - UFR des Sciences et des Techniques (UN UFR ST), Université de Nantes (UN)-Université de Nantes (UN)-Institut Universitaire de Technologie Saint-Nazaire (IUT Saint-Nazaire), Université de Nantes (UN)-Ecole Polytechnique de l'Université de Nantes (EPUN), Université de Nantes (UN)-École nationale vétérinaire, agroalimentaire et de l'alimentation Nantes-Atlantique (ONIRIS)-Centre National de la Recherche Scientifique (CNRS)-Université Bretagne Loire (UBL)-IMT Atlantique (IMT Atlantique), Institut Mines-Télécom Paris (IMT)-Institut Mines-Télécom Paris (IMT)-Institut Universitaire de Technologie - La Roche-sur-Yon (IUT La Roche-sur-Yon), Université de Nantes (UN)

المصدر: Innovations in Food Science & Technology ; https://hal.science/hal-01497614Test ; Innovations in Food Science & Technology, May 2017, Munich, Germany

مصطلحات موضوعية: industrie agroalimentaire, Beta-Lactoglobuline, nature conservation, whey protein, lactotransferrin, ²-lactoglobulin, conservation, protéine de lactosérum, vitamine, coacervation, lactoferrine, beta lactoglobuline, [SDV.AEN]Life Sciences [q-bio]/Food and Nutrition, [SDV.IDA]Life Sciences [q-bio]/Food engineering

جغرافية الموضوع: Munich, Germany

الوصف: The production of natural biocarriers for the protection and controlled delivery of bioactives is of great interest to develop natural functional foods, with enhanced health benefits. The feasibility of heteroprotein complex coacervates formed between two whey proteins (WP), Beta-Lactoglobulin (BLG) and Lactoferrin (LF) to efficiently entrap vitamin B9 has been demonstrated. In the present communication, we investigated the bench scale production of such B9 loaded BLG-LF coacervates (B9-WP coacervates) and their protective ability against B9 degradations during storage (freeze-drying, UV light radiations and accelerated H2O2 induced oxidation). Complex coacervation was performed at bench scale, using commercial protein solutions. The efficiency of two mixing systems, batch versus continuous, were compared. In the continuous mixing system, the formation of B9-WP coacervates was found to be flow-dependant (Figure 1). The highest WP coacervation yield was obtained for a minimum flow rate of 200 mL/min. Under optimized conditions, bench scale efficiency similar to that found for laboratory scale was reached with a coacervation yield of 65 % and a B9 entrapment of 98 %, demonstrating an efficient scaling-up. When entrapped into WP coacervates B9 showed higher stability during freeze-drying with a loss of about 3%, compared to 12% obtained for free unentrapped B9. Additionally, WP coacervates showed good protective effect of B9 against UV irradiation and H2O2 induced oxidation. Hence, heteroprotein complex coacervates constitute a promising biocarriers for the protection of bioactives against chemical and physical degradation. For controlled delivery purpose, in vitro and in vivo studies are in progress to evaluate the effectiveness and optimal release of entrapped B9 molecules. The production of natural biocarriers for the protection and controlled delivery of bioactives is of great interest to develop natural functional foods, with enhanced health benefits. The feasibility of heteroprotein complex coacervates formed ...

العلاقة: hal-01497614; https://hal.science/hal-01497614Test; PRODINRA: 389670

الإتاحة: https://hal.science/hal-01497614Test

المؤلفون: Chapeau, Anne Laure

المساهمون: Science et Technologie du Lait et de l'Oeuf (STLO), Institut National de la Recherche Agronomique (INRA)-AGROCAMPUS OUEST, Institut National de Recherche Agronomique (INRA). UMR UMR INRA / AgroCampus Rennes : Science et Technologie du Lait et de l'?uf (1253).

المصدر: Journée PROFIL - La plasticité des protéines du lait : un atout majeur pour concevoir des assemblages fonctionnels ; https://hal.science/hal-01595711Test ; Journée PROFIL - La plasticité des protéines du lait : un atout majeur pour concevoir des assemblages fonctionnels, Institut National de Recherche Agronomique (INRA). UMR UMR INRA / AgroCampus Rennes : Science et Technologie du Lait et de l'?uf (1253)., Sep 2017, Rennes, France ; https://journees.inra.fr/profil/ProgrammeTest

مصطلحات موضوعية: milk protein, protéine laitière, protéine du lait, protéine sérique, vitamine b9, molécule bioactive, technologie laitière, coacervation, encapsulation, [SDV.AEN]Life Sciences [q-bio]/Food and Nutrition, [SDV.IDA]Life Sciences [q-bio]/Food engineering

جغرافية الموضوع: Rennes, France

الوصف: Les protéines du lait constituent une véritable malle au trésor. Les avancées scientifiques actuelles sur le lait mettent de plus en plus en exergue la plasticité des protéines laitières, souvent décrites comme l’or blanc du lait. La capacité de ces protéines à former des assemblages aptes à fonctionnaliser des interfaces, eau-huile et eau-air, pour obtenir des émulsions et des mousses ; à texturer les produits ou encore à vectoriser des molécules d’intérêt offre un énorme potentiel d’innovation. Ce potentiel s’inscrit dans la tendance du Clean Label et la création de nouveaux produits laitiers 100% lait.Le projet PROFIL (PROtéines Fonctionnalisées pour l’Industrie Laitière) a été bâti sur ces extraordinaires découvertes. Il réunit sept partenaires académiques et un consortium de 10 industriels laitiers regroupés au sein du consortium BBA.L’objectif de la journée du 21 septembre est de partager avec les chercheurs, académiques et industriels les résultats marquants de PROFIL qui seront présentés par six doctorants.

العلاقة: hal-01595711; https://hal.science/hal-01595711Test; https://hal.science/hal-01595711/documentTest; https://hal.science/hal-01595711/file/20170921_ColloqPROFIL_sept2017_ALChapeau-Axe4_1.pdfTest; PRODINRA: 408760

الإتاحة: https://hal.science/hal-01595711Test
https://hal.science/hal-01595711/documentTest
https://hal.science/hal-01595711/file/20170921_ColloqPROFIL_sept2017_ALChapeau-Axe4_1.pdfTest

المؤلفون: Boire, Adeline, Bouchoux, Antoine, Bouhallab, Said, Chapeau, Anne Laure, Croguennec, Thomas, Ferraro, Vincenza, Lechevalier-Datin, Valérie, Menut, Paul, Pezennec, Stephane, Renard, Denis, Santé-Lhoutellier, Véronique, Laleg, Karima, Micard, Valerie, Riaublanc, Alain, Anton, Marc

المساهمون: Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA), Institut National de la Recherche Agronomique (INRA), Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés (LISBP), Institut National de la Recherche Agronomique (INRA)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS), Science et Technologie du Lait et de l'Oeuf (STLO), Institut National de la Recherche Agronomique (INRA)-AGROCAMPUS OUEST, Qualité des Produits Animaux (QuaPA), Ingénierie, Procédés, Aliments (GENIAL), Institut National de la Recherche Agronomique (INRA)-AgroParisTech, Ingénierie des Agro-polymères et Technologies Émergentes (UMR IATE), Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Institut National de la Recherche Agronomique (INRA)-Université Montpellier 2 - Sciences et Techniques (UM2)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Université de Montpellier (UM)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), European Project: 609398,EC:FP7:PEOPLE,FP7-PEOPLE-2013-COFUND,AGREENSKILLSPLUS(2014)

المصدر: ISSN: 1466-8564.

مصطلحات موضوعية: new technology, surface properties, intermolecular interaction, protein, innovation, valorisation des sous produits, interaction protéine protéine, hétéroprotéine, propriété de surface, interaction intermoléculaire, caséine micellaire, gliadine, lysozyme, protéine, aliment enrichi, encapsulation, [SDV.IDA]Life Sciences [q-bio]/Food engineering

الوصف: Proteins for the future: A soft matter approach to link basic knowledge and innovative applications

العلاقة: info:eu-repo/grantAgreement/EC/FP7/609398/EU/AgreenSkills+/AGREENSKILLSPLUS; hal-01608238; https://hal.science/hal-01608238Test; https://hal.science/hal-01608238/documentTest; https://hal.science/hal-01608238/file/Boire-IFSET-2017-manuscript-IATE_1.pdfTest; PRODINRA: 397542; WOS: 000435059500003

الإتاحة: https://doi.org/10.1016/j.ifset.2017.06.012Test
https://hal.science/hal-01608238Test
https://hal.science/hal-01608238/documentTest
https://hal.science/hal-01608238/file/Boire-IFSET-2017-manuscript-IATE_1.pdfTest

المؤلفون: Casanova, Federico, Chapeau, Anne Laure, Hamon, Pascaline, de Carvalho, Antonio F., Croguennec, Thomas, Bouhallab, Said

المساهمون: Science et Technologie du Lait et de l'Oeuf (STLO), Institut National de la Recherche Agronomique (INRA)-AGROCAMPUS OUEST, Laboratory of Research in Milk Products, Universidade Federal de Viçosa = Federal University of Viçosa (UFV)

المصدر: ISSN: 0308-8146.

مصطلحات موضوعية: Sodium caseinate, Cyanidin-3-O-glucoside, Thermodynamic analysis, Fluorescence spectroscopy, protein, spectroscopie à fluorescence, molécule bioactive, caséinate de sodium, cyanidine, glucoside, protéine, interaction, [SDV.AEN]Life Sciences [q-bio]/Food and Nutrition, [SDV.IDA]Life Sciences [q-bio]/Food engineering

الوصف: International audience ; Understanding the mechanism of interaction between food proteins and bioactives constitutes the preliminarystep to design food grade nanocarriers. We investigated the interaction between cyanidin-3-O-glucoside (C3G), and 20 nm-sized sodium caseinate nanoparticles (NaCas) at pH 7 and pH 2 byfluorescence spectroscopy and dynamic light scattering. The characterization of the C3G-NaCas interactionindicated that the fluorescence quenching mechanism was predominantly static. C3G interactedwith two sets of binding sites with association constants Ka of 106 and 105 M 1. Electrostatic interactionsdominated at pH 7, while hydrophobic effects were the main force at pH 2. Interestingly, the two sets ofbinding sites were discriminated by ionic strength at pH 7. The binding of C3G slightly modified theaverage diameter of NaCas nanoparticles without alteration of its surface charge suggesting a complexationof C3G molecules in the internal casein structure. Thus, NaCas constitutes a putative nanocarrier foranthocyanins in new functional foods.

العلاقة: hal-01574202; https://hal.science/hal-01574202Test; PRODINRA: 403741; WOS: 000436897900008

الإتاحة: https://doi.org/10.1016/j.foodchem.2017.06.081Test
https://hal.science/hal-01574202Test

المؤلفون: Chapeau, Anne Laure, Hamon, Pascaline, Rousseau, Florence, Croguennec, Thomas, Poncelet, Denis, Bouhallab, Said

المساهمون: Science et Technologie du Lait et de l'Oeuf (STLO), Institut National de la Recherche Agronomique (INRA)-AGROCAMPUS OUEST, Laboratoire de génie des procédés - environnement - agroalimentaire (GEPEA), Institut Universitaire de Technologie - Nantes (IUT Nantes), Université de Nantes (UN)-Université de Nantes (UN)-Université de Nantes - UFR des Sciences et des Techniques (UN UFR ST), Université de Nantes (UN)-Université de Nantes (UN)-Institut Universitaire de Technologie Saint-Nazaire (IUT Saint-Nazaire), Université de Nantes (UN)-Ecole Polytechnique de l'Université de Nantes (EPUN), Université de Nantes (UN)-École nationale vétérinaire, agroalimentaire et de l'alimentation Nantes-Atlantique (ONIRIS)-Centre National de la Recherche Scientifique (CNRS)-Université Bretagne Loire (UBL)-IMT Atlantique (IMT Atlantique), Institut Mines-Télécom Paris (IMT)-Institut Mines-Télécom Paris (IMT)-Institut Universitaire de Technologie - La Roche-sur-Yon (IUT La Roche-sur-Yon), Université de Nantes (UN), Regional councils of Brittany (grant n 13008651) and Pays de la Loire (grant n 2014-07081) and INRA for the financial support of this work through the interregional project PROFIL, supported by BBA industrial association and managed by the “P^ole Agronomique Ouest”.

المصدر: ISSN: 0260-8774 ; Journal of Food Engineering ; https://hal.science/hal-01506631Test ; Journal of Food Engineering, 2017, 206, pp.67-76. ⟨10.1016/j.jfoodeng.2017.03.005⟩.

مصطلحات موضوعية: nature conservation, whey protein, lactotransferrin, ²-lactoglobulin, vitamine b9, lactoferrine, beta lactoglobuline, molécule bioactive, industrie agro-alimentaire, coacervation, encapsulation, conservation, protéine de lactosérum, [SDV.AEN]Life Sciences [q-bio]/Food and Nutrition, [SDV.IDA]Life Sciences [q-bio]/Food engineering

الوصف: The production of biocarriers for the protection and controlled delivery of bioactives is of great interest todevelop functional foods. The ability of two whey proteins (WP), Beta-Lactoglobulin (BLG) and Lactoferrin(LF), to efficiently entrap vitamin B9 by complex coacervation has been reported at laboratoryscale. In the present work, we report on the scaling-up production of B9 loaded BLG-LF coacervates (B9-WP coacervates). Complex coacervation was performed at bench scale, using commercial protein solutions.Under optimized conditions, B9-WP coacervates were produced by static mixing at a flow rate of300 mL/min. Bench scale efficiency similar to that found for laboratory scale was reached with a coacervationyield of 65% and the B9 entrapment of 98%, demonstrating an efficient scaling-up. B9-WP coacervatesshowed good protection property for B9 during storage treatments, confirming the efficiency ofthis type of biocarrier for the development of natural functional foods.

العلاقة: hal-01506631; https://hal.science/hal-01506631Test; PRODINRA: 390419; WOS: 000400215900007

الإتاحة: https://doi.org/10.1016/j.jfoodeng.2017.03.005Test
https://hal.science/hal-01506631Test

المؤلفون: Chapeau, Anne Laure, Bertrand, Nicolas, Briard-Bion, Valérie, Hamon, Pascaline, Poncelet, Denis, Bouhallab, Said

المساهمون: Science et Technologie du Lait et de l'Oeuf (STLO), Institut National de la Recherche Agronomique (INRA)-AGROCAMPUS OUEST, Laboratoire de génie des procédés - environnement - agroalimentaire (GEPEA), Institut Universitaire de Technologie - Nantes (IUT Nantes), Université de Nantes (UN)-Université de Nantes (UN)-Université de Nantes - UFR des Sciences et des Techniques (UN UFR ST), Université de Nantes (UN)-Université de Nantes (UN)-Institut Universitaire de Technologie Saint-Nazaire (IUT Saint-Nazaire), Université de Nantes (UN)-Ecole Polytechnique de l'Université de Nantes (EPUN), Université de Nantes (UN)-École nationale vétérinaire, agroalimentaire et de l'alimentation Nantes-Atlantique (ONIRIS)-Centre National de la Recherche Scientifique (CNRS)-Université Bretagne Loire (UBL)-IMT Atlantique (IMT Atlantique), Institut Mines-Télécom Paris (IMT)-Institut Mines-Télécom Paris (IMT)-Institut Universitaire de Technologie - La Roche-sur-Yon (IUT La Roche-sur-Yon), Université de Nantes (UN), Faculty of Pharmacy, CHU de Quebec Research Center, Université Laval Québec (ULaval), Institute of Nutrition and Functional Foods INAF, Regional councils of Brittany (grant n 13008651) and Pays de la Loire (grant n 2014-07081) and INRA, France for the financial support of this work through the interregional project PROFIL, supported by BBA industrial association and managed by the ‘‘Pôle Agronomique Ouest”. Additional funding from the Natural Sciences and Engineering Research Council of Canada (Discovery Grant to N. B.)

المصدر: ISSN: 1756-4646.

مصطلحات موضوعية: protection, formulation, drug kinetics, vitamine b9, molécule bioactive, coacervation, encapsulation, pharmacocinétique, bioaccessibilité, formulation alimentaire, matrice alimentaire, [SDV.AEN]Life Sciences [q-bio]/Food and Nutrition, [SDV.IDA]Life Sciences [q-bio]/Food engineering

الوصف: The potentiality of heteroprotein complex coacervates as biocarrier for a bioactive was investigated.Vitamin B9 (B9), also known as folic acid, was encapsulated by complex coacervation of two whey proteins(WP), b-lactoglobulin and lactoferrin. The stability and bioavailability of formed B9-WP coacervateswas then characterized. Under degradative conditions in vitro (UV light irradiation, and oxidation byH2O2), WP coacervates protected the vitamin against chemical degradation. B9-WP coacervates alsoshowed considerable physical stability over time when incorporated in real food matrices. Comparedto unencapsulated B9, oral administration of B9-WP coacervates to healthy rats enhanced the plasmalevel of the vitamin. This improved bioavailability can be ascribed to the improvement in the solubilityof B9 throughout the gastro-intestinal tract. We thus demonstrate the efficiency of WP coacervates asbiocarrier for the protection and delivery of small bioactive molecules.

العلاقة: hal-01593201; https://hal.science/hal-01593201Test; https://hal.science/hal-01593201/documentTest; https://hal.science/hal-01593201/file/ALC_JFF_2017_%7BB33A7091-A159-48D5-83E3-5A117834388A%7D.pdfTest; PRODINRA: 408659; WOS: 000414890500019

الإتاحة: https://doi.org/10.1016/j.jff.2017.09.009Test
https://hal.science/hal-01593201Test
https://hal.science/hal-01593201/documentTest
https://hal.science/hal-01593201/file/ALC_JFF_2017_%7BB33A7091-A159-48D5-83E3-5A117834388A%7D.pdfTest

المؤلفون: Chapeau, Anne Laure, Miranda-Tavares, Guilherme, Hamon, Pascaline, Croguennec, Thomas, Bouhallab, Said, Poncelet, Denis

المساهمون: Science et Technologie du Lait et de l'Oeuf (STLO), Institut National de la Recherche Agronomique (INRA)-AGROCAMPUS OUEST, Laboratory Research in Milk Products, Universidade Federal de Viçosa = Federal University of Viçosa (UFV), Laboratoire de génie des procédés - environnement - agroalimentaire (GEPEA), Mines Nantes (Mines Nantes)-Université de Nantes - UFR des Sciences et des Techniques (UN UFR ST), Université de Nantes (UN)-Université de Nantes (UN)-École nationale vétérinaire, agroalimentaire et de l'alimentation Nantes-Atlantique (ONIRIS)-Centre National de la Recherche Scientifique (CNRS)

المصدر: 23.International Conference on Bioencapsulation
https://hal.science/hal-01209845Test
23.International Conference on Bioencapsulation, Sep 2015, Delft, Netherlands. , 2015
https://archives-publications.inrae.fr/310426.pdfTest

مصطلحات موضوعية: assemblage de protéine, fonctionnalité des protéines, encapsulation, vitamine hydrophile, coacervation, [SDV.AEN]Life Sciences [q-bio]/Food and Nutrition, [SDV.IDA]Life Sciences [q-bio]/Food engineering

جغرافية الموضوع: Delft, Netherlands

الوصف: Encapsulation of bioactive compounds such as vitamins and micronutrients is a great challenge to develop new functional foods. There is a growing demand from consumers for food products offering health benefits such as products enriched with vitamins. At the same time, consumers tend to favor natural food or products with minimal amount of additives. The encapsulation of bioactives usually resorts to extraneous components that are not natural constituents of the targeted food product. It could therefore be relevant to seek to encapsulate bioactive molecules by means of intraneous components that are natural constituents of the targeted food product.Among food constituents, food proteins are biopolymers that appear suitable for the transport and protection of several bioactives. Recent studies have reported the ability of two oppositely charged milk proteins, beta-lactoglobulin (BLG) and lactoferrin (LF), to spontaneously co-assemble to form heteroprotein complexes called “coacervates” (Anema et al., 2014; Tavares et al., 2015). Complex coacervation is a well-known phase separation between two oppositely charged macromolecules, into a concentrated phase of coacervates and dilute phase. It can be used as an encapsulation technique. In the literature, two general procedures can be found to encapsulate a compound by the complex coacervation of two biopolymers.The objective of this work is to investigate the potentialities of coacervates entirely made from food proteins to encapsulate a bioactive compound according to these procedures. We investigated the potentiality of BLG-LF coacervates to encapsulate the hydrophilic vitamin B9

العلاقة: hal-01209845; https://hal.science/hal-01209845Test; https://hal.science/hal-01209845/documentTest; https://hal.science/hal-01209845/file/AL-Chapeau_Abstract_BioencapsulationCongress_201506_1.pdfTest; PRODINRA: 310426

الإتاحة: https://hal.science/hal-01209845Test
https://hal.science/hal-01209845/documentTest
https://hal.science/hal-01209845/file/AL-Chapeau_Abstract_BioencapsulationCongress_201506_1.pdfTest

المؤلفون: Bouhallab, Said, Miranda-Tavares, Guilherme, Chapeau, Anne Laure, Hamon, Pascaline, Croguennec, Thomas

المساهمون: Science et Technologie du Lait et de l'Oeuf (STLO), Institut National de la Recherche Agronomique (INRA)-AGROCAMPUS OUEST

المصدر: Journées scientifiques Matière molle pour la science des aliments : Compréhension et Structuration ; https://hal.science/hal-01454546Test ; Journées scientifiques Matière molle pour la science des aliments : Compréhension et Structuration, Oct 2015, Montpellier, France

مصطلحات موضوعية: assemblage de protéine, joining processes, protein, coacervation, assemblage, encapsulation, protéine, propriété physicochimique, molécule bioactive, [SDV.AEN]Life Sciences [q-bio]/Food and Nutrition, [SDV.IDA]Life Sciences [q-bio]/Food engineering

جغرافية الموضوع: Montpellier, France

الوصف: The application of fundamental physicochemical concepts for rational design of functional assemblies fromfood proteins constitute a response to the growing trend toward the development of new and in novative food products and also an opportunity to generate new protein -based supramolecular structures with new applications. Because of their omnipresence in food systems and their biodegradability, proteins are the focus of many attempts for their use as building blocks for such supramolecular structures. Controlled self-co-assembly of proteins can generate a variety of supramolecular structures that vary in shape, size and density (fibrils, spherulites, nanotubes, etc). For instance, coacervates can be formedin heteroprotein systems by control mixing of oppositely charged proteins.1The objective of our research is to understand the mechanisms behind such spontaneous coacervation process frommolecular interaction to micro-scale characterization. In this presentation, we will summarize the results obtained on several binary protein systems and will show that co-assembly of proteins into coacervates (Figure 1) is a generic process that is, de facto, independent of the amino acid composition. We will report on the requirements that drive such spontaneous co-assembly: protein conformational state and flexibility, molar stoichiometry, total protein concentration, charge anisotropy, etc. Mention will be made to the research challenges and the promising uses of these supramolecular structures in food and non-food sectors (encapsulation of bioactives, design of edible films).

العلاقة: hal-01454546; https://hal.science/hal-01454546Test; https://hal.science/hal-01454546/documentTest; https://hal.science/hal-01454546/file/Bouhallab_1Test; PRODINRA: 331901

الإتاحة: https://hal.science/hal-01454546Test
https://hal.science/hal-01454546/documentTest
https://hal.science/hal-01454546/file/Bouhallab_1Test