8 results on '"Marion Morand"'
Search Results
2. Automatic Extraction of a Piecewise Symmetry Surface of a 3D Mesh: Application to Scoliosis.
- Author
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Marion Morand, Olivier Comas, Gérard Subsol, and Christophe Fiorio
- Published
- 2018
- Full Text
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3. Automatic extraction of the 3D symmetry line of back surface: application on scoliotic adolescents
- Author
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Olivier Comas, Gérard Subsol, Christophe Fiorio, Marion Morand, Image & Interaction (ICAR), Laboratoire d'Informatique de Robotique et de Microélectronique de Montpellier (LIRMM), Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM), DMS Imaging, and IEEE
- Subjects
2. Zero hunger ,Surface (mathematics) ,Adolescent ,[INFO.INFO-CV]Computer Science [cs]/Computer Vision and Pattern Recognition [cs.CV] ,Geometry ,Scoliosis ,Surface symmetry ,Back surface topography ,Symmetry line ,medicine.disease ,[INFO.INFO-GR]Computer Science [cs]/Graphics [cs.GR] ,030218 nuclear medicine & medical imaging ,Automation ,03 medical and health sciences ,0302 clinical medicine ,Spinous process line ,Local symmetry ,medicine ,[INFO.INFO-IM]Computer Science [cs]/Medical Imaging ,Humans ,Reference line ,030217 neurology & neurosurgery ,Mathematics - Abstract
International audience; We propose a new method to extract automatically the symmetry line of the 3D back surface of patients affected by scoliosis. Our method is based on the detection of local symmetry planes computed on thick layers of the back. Results have been obtained on a sample of 112 scoliotic adolescents and we compare the symmetry line obtained by our method with a reference line defined by clinicians. We also study the influence of the scoliosis severity and of the Body Mass Index on the results.
- Published
- 2018
4. A Rapid Electrophoresis Method on Agarose Gel to Characterise Dairy Protein Aggregates
- Author
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Yann Demarigny, Laetitia Gemelas, Marion Morand, Pascal Degraeve, Arnaud Hallier, Bioingénierie et Dynamique Microbienne aux Interfaces Alimentaires (BIODYMIA), Isara-Université Claude Bernard Lyon 1 (UCBL), and Université de Lyon-Université de Lyon
- Subjects
2. Zero hunger ,Chromatography ,Chemistry ,food and beverages ,Dairy industry ,Protein aggregation ,Electrophoresis ,chemistry.chemical_compound ,fluids and secretions ,Agarose gel electrophoresis ,[SDV.IDA]Life Sciences [q-bio]/Food engineering ,Agarose ,Composition (visual arts) ,Protein spot - Abstract
Heat treatment of milk may cause whey proteins and caseins to form aggregates. These soluble and micellar aggregates and their other properties (size, composition, shape, etc.) can affect the techno-functionalities to the milk, conferring interesting or negative features depending on the application in dairy industries. In this study, we propose a new approach to characterise those protein aggregates. SDS-agarose electrophoresis is followed by the calculation of a retention factor (Rf) for each protein spot. Rf allows milk aggregates to be compared qualitatively under the same conditions. This method could be transposed to the dairy industry for a better knowledge of the milk subsequent to heat treatment.
- Published
- 2018
5. Increasing the hydrophobicity of the heat-induced whey protein complexes improves the acid gelation of skim milk
- Author
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Fanny Guyomarc'H, Assiba Dekkari, Marie-Hélène Famelart, Marion Morand, Science et Technologie du Lait et de l'Oeuf (STLO), Institut National de la Recherche Agronomique (INRA)-AGROCAMPUS OUEST, Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro), and Région Bretagne, ARED 4298
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[SDV.SA]Life Sciences [q-bio]/Agricultural sciences ,Whey protein ,Heat induced ,food.ingredient ,gelation ,Applied Microbiology and Biotechnology ,Hydrophobic effect ,Acylation ,0404 agricultural biotechnology ,food ,fluids and secretions ,Skimmed milk ,chemistry.chemical_classification ,Carbon chain ,Chromatography ,0402 animal and dairy science ,food and beverages ,04 agricultural and veterinary sciences ,040401 food science ,040201 dairy & animal science ,lait ,hydrophobicité ,Isoelectric point ,chemistry ,protéine ,Thiol ,Food Science ,traitement thermique - Abstract
The formation of whey protein complexes during heating enhances the acid gelation of milk; hydrophobic interactions may play an important role in this acid gelation. To investigate this, the surface hydrophobicity of model heat-induced whey protein complexes was modified using acylation with various carbon chain lengths. It was determined that the size and thiol/disulfide distribution of the complexes were unaffected, and that the change in their apparent isoelectric point could be restricted within 0.5 pH unit. These complexes were added to whey protein-free skim milk systems and the resulting acid-gelation behaviour of the milk samples was measured. Increasing the hydrophobicity of the heat-induced whey protein complexes significantly increased the pH of gelation of the milk samples and strongly affected the final properties of the acid gels, demonstrating both the importance of the heat-induced complexes and the relevance of hydrophobic interactions in the acid-induced gelation of preheated milk.
- Published
- 2012
6. Agrégation protéique et propriétés gélifiantes et moussantes des protéines laitières ; Quoi de neuf sur le plan des connaissances ?
- Author
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Marie-Hélène Famelart, Fanny Guyomarc'H, Marion Morand, Bruno Novales, Science et Technologie du Lait et de l'Oeuf (STLO), Institut National de la Recherche Agronomique (INRA)-AGROCAMPUS OUEST, Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA), Institut National de la Recherche Agronomique (INRA), and Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)
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[SDV.SA]Life Sciences [q-bio]/Agricultural sciences ,β-LACTOGLOBULINE ,product processing ,chauffage ,heating ,proteine laitiere ,FOAM ,²-lactoglobulin ,moss ,transformation des produits ,milk protein ,protéine du lait ,[SDV.IDA]Life Sciences [q-bio]/Food engineering ,gel acide ,jellification ,TEMPERATURE ,yoghurt ,GEL ,PROTEIN AGGREGATE ,milk ,beta lactoglobuline ,AGREGAT PROTEIQUE ,LAIT ,MOUSSE ,PROTEINE ,AGREGATION ,TRAITEMENT ,YAOURT ,MILK ,BETA-LACTOGLOBULIN ,agrégat protéique lait gel mousse β-lactoglobuline ,yaourt ,lait ,traitement thermique de l'aliment ,Agricultural sciences ,mousse ,protéine ,propriété physicochimique ,aggregates ,agrégat ,protein ,[SDV.AEN]Life Sciences [q-bio]/Food and Nutrition ,Sciences agricoles ,gélification ,traitement thermique - Abstract
During the manufacture of dairy products, heat treatments of milk result in the conversion of whey proteins into protein aggregates. These heat-induced aggregates provide new functional properties to dairy products. A protein tailoring approach is developed at UMR-STLO to produce heat-induced aggregates with targeted physicochemical and structural properties, and then to introduce them in a recombined milk to test their functional properties for the formation of dairy acid gels, used as models of yoghurts. It is also well known that denaturation and heat treatments improve interfacial and foaming properties of proteins. The BIA research unit works on understanding the role of heat-induced aggregates in the formation and stability of foams. While non-aggregated proteins adsorb rapidly at the interface, the heat-induced aggregates present in the continuous phase build a protein network that stabilizes the foam. The objective of theses studies is to determine the properties of aggregates that promote the building of new interactions in products that will result in the improvement of custom properties of dairy products and to produce new functional ingredients.; formation de nouvelles entités protéiques ou agrégats thermo-induits. Ces agrégats confèrent des propriétés fonctionnelles aux produits laitiers. Une approche d’ingénierie des agrégats thermo-induits a été développée à l’UMR-STLO qui vise à produire par des moyens variés des agrégats thermo-induits de propriétés physico-chimiques et structurales ciblées, puis à les introduire dans un lait recombiné afin d’évaluer leur propriétés fonctionnelles pour la formation des gels acides, pris comme un modèle du yaourt. Il est connu que la dénaturation et les traitements thermiques améliorent également les propriétés interfaciales et moussantes des protéines. Le laboratoire BIA mène des recherches pour comprendre le rôle des agrégats thermo-induits dans la formation et la stabilisation des mousses. Alors que les protéines non agrégées s’adsorbent rapidement à l’interface, la présence d’agrégats thermoinduits stabilise la mousse par formation d’un réseau de type gel dans la phase continue. L’objectif de ces travaux est de déterminer les propriétés des agrégats qui sont favorables à l’établissement de nouvelles interactions dans les produits, ces dernières étant à l’origine de l’amélioration de leurs propriétés d’usage et de créer de nouveaux ingrédients techno-fonctionnels.
- Published
- 2011
7. How to tailor heat-induced whey protein/κ-casein complexes as a means to investigate the acid gelation of milk--a review
- Author
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Marie-Hélène Famelart, Marion Morand, Fanny Guyomarc'H, and Region Bretagne (ARED 4298)
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WHEY PROTEINS ,Whey protein ,Heat induced ,Globular protein ,PROTEIN ,Dairy industry ,Retention capacity ,01 natural sciences ,Biochemistry ,CHAUFFAGE ,0404 agricultural biotechnology ,fluids and secretions ,MILK ,Casein ,YAOURT ,PROTEINE ,[SDV.IDA]Life Sciences [q-bio]/Food engineering ,REVIEW ,HEAT TREATMENT ,Food science ,LAIT ,GELATION ,REVUE ,YOGHURT ,ACID GEL ,COMPLEX ,CASEIN ,chemistry.chemical_classification ,caséine ,Chemistry ,010401 analytical chemistry ,Heated milk ,food and beverages ,04 agricultural and veterinary sciences ,040401 food science ,Casein micelles ,0104 chemical sciences ,Agricultural sciences ,protéine ,[SDV.AEN]Life Sciences [q-bio]/Food and Nutrition ,Sciences agricoles ,Food Science - Abstract
The heat treatment of milk greatly improves the acid gelation of milk and is therefore largely applied in yoghurt manufacture. During the heat treatment, soluble and micelle-bound whey protein/κ-casein complexes are produced in milk. The complexes and their physico-chemical properties have been held responsible for the early gelation point, the increased final firmness and for the serum retention capacity of the acid gels made of heated milk. They are suspected to bring new functionalities to the casein micelles and to help the formation of interactions when building the gel network. In order to investigate the type of interactions that the complexes can affect throughout the acid gelation of milk, an original strategy would be to control the physico-chemical properties of the whey protein/κ-casein soluble complexes and to use them as vectors to modify the possible interactions in the milk. In that perspective, the different physico-chemical properties of the whey protein/κ-casein soluble complexes that are thought to significantly affect the acid gelation behaviour of the casein micelles are listed. Then, the physical, chemical and biological means that could possibly be applied to the formation of complexes in order to modulate each of the targeted property are reviewed and evaluated. In order to open a large choice for future investigation, these methods were found in a larger literature resource than milk, including other protein systems like model whey protein solutions or non-dairy globular protein systems. The food-compatible character of some of these means is indicated, for their potential technological interest.
- Published
- 2011
8. On how k-casein affects the interactions between the heat-induced whey protein/k-casein complexes and the casein micelles during the acid gelation of skim milk
- Author
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Fanny Guyomarc'H, Marie-Hélène Famelart, Marion Morand, Stéphane Pezennec, Science et Technologie du Lait et de l'Oeuf (STLO), Institut National de la Recherche Agronomique (INRA)-AGROCAMPUS OUEST, Région Bretagne (grant ARED 4298), rench Research Agency (ANR), European Union, Région Bretagne, Rennes Métropole, Conseil Général 35, and Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)
- Subjects
[SDV.SA]Life Sciences [q-bio]/Agricultural sciences ,Whey protein ,Heat induced ,food.ingredient ,animal structures ,Applied Microbiology and Biotechnology ,Micelle ,0404 agricultural biotechnology ,food ,fluids and secretions ,milk protein ,protéine du lait ,Casein ,Skimmed milk ,Food science ,Protein secondary structure ,chemistry.chemical_classification ,milk ,Chromatography ,0402 animal and dairy science ,food and beverages ,04 agricultural and veterinary sciences ,040401 food science ,040201 dairy & animal science ,Casein micelles ,lait ,chemistry ,protéine ,Thiol ,protein ,INTERACTION ,Food Science ,traitement thermique - Abstract
Heat treatment of milk at 85–95 °C has long been reported to increase the pH of gelation and firmness of acid milk gels; hence its wide application in yoghurt manufacture. These changes have been attributed to the formation of heat-induced whey protein/κ-casein complexes in the milk, to which heat-denatured whey protein ingredients may be substituted. However, variations in resulting gels show that a possible role of κ-casein in determining the functional acid-gelation property of the complexes needs investigating. Model heat-induced whey protein/κ-casein complexes were produced of κ-casein content from 0 to 40% (w/w), but of similar size, secondary structure, surface hydrophobicity and thiol/disulphide distribution. These complexes were added to whey protein-free skim milk systems and the resulting acid-gelation behaviour of the milks was evaluated. The results showed a modification of the pH of gelation that was explained more by variation of the pI of complexes than by the κ-casein content.
- Published
- 2011
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