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25. Conformational stability and binding properties of porcine odorant binding protein

Author

Burova, Tatiana, Choiset, Yvan, Jankowski, Christophe K., and Haertle, Thomas

Subjects
Cytochemistry -- Research, Carrier proteins -- Physiological aspects, Smell -- Research, Swine -- Physiological aspects, Calorimetry -- Usage, Biological sciences, Chemistry
Abstract

Porcine odorant binding protein (pOBP) is discussed relative to its conformational stability and binding properties. Results of thermodynamic study by high-sensitivity differential scanning calorimetry and isothermal titration calorimetry indicate that the mechanism of binding to pOBP of the odorants studied is not primarily a hydrophobic process related to any change in protein hydration. Likely it is driven by polar and van der Waals interactions.

Published
1999

34. Microwave processing assisted enzymatic digestion: a new approach for the reduction of whey protein and b-lactoglobulin allergenicity

Author

El Mecherfi, Kamel Eddine, Curet, Sébastien, Lupi, Roberta, Larre, Colette, Rouaud, Olivier, Choiset, Yvan, Rabesona, Hanitra, Haertlé, T, Laboratoire de Physiologie de la Nutrition et Sécurité Alimentaire, Département de Biologie, Faculté des Sciences, Université Oran 1 Ahmed Ben Bella, Optimisation - Système - Energie (GEPEA-OSE), Laboratoire de génie des procédés - environnement - agroalimentaire (GEPEA), Ecole Nationale Vétérinaire, Agroalimentaire et de l'alimentation Nantes-Atlantique (ONIRIS)-Université Bretagne Loire (UBL)-IMT Atlantique Bretagne-Pays de la Loire (IMT Atlantique), Institut Mines-Télécom [Paris] (IMT)-Institut Mines-Télécom [Paris] (IMT)-Université de Nantes (UN)-Centre National de la Recherche Scientifique (CNRS)-Ecole Nationale Vétérinaire, Agroalimentaire et de l'alimentation Nantes-Atlantique (ONIRIS)-Université Bretagne Loire (UBL)-IMT Atlantique Bretagne-Pays de la Loire (IMT Atlantique), Institut Mines-Télécom [Paris] (IMT)-Institut Mines-Télécom [Paris] (IMT)-Université de Nantes (UN)-Centre National de la Recherche Scientifique (CNRS), Ecole Nationale Vétérinaire, Agroalimentaire et de l'alimentation Nantes-Atlantique (ONIRIS), Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA), Institut National de la Recherche Agronomique (INRA), UMR1268, Biopolymères, Interactions Assemblages (BIA), 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)-Ecole Nationale Vétérinaire, Agroalimentaire et de l'alimentation Nantes-Atlantique (ONIRIS)-Centre National de la Recherche Scientifique (CNRS)-Université Bretagne Loire (UBL)-IMT Atlantique Bretagne-Pays de la Loire (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)-Institut Universitaire de Technologie - Nantes (IUT Nantes), and Université de Nantes (UN)

Subjects
[SPI]Engineering Sciences [physics], [SPI.GPROC]Engineering Sciences [physics]/Chemical and Process Engineering, [SDV.AEN]Life Sciences [q-bio]/Food and Nutrition, ComputingMilieux_MISCELLANEOUS
Abstract

International audience

Published
2017

35. Physicochemical, microbiological characterization and proteolysis of Algerian traditional Bouhezza cheese prepared from goat's raw milk.

Author

Medjoudj, Hacène, Aouar, Lamia, Derouiche, Meriem, Choiset, Yvan, Haertlé, Thomas, Chobert, Jean-Marc, Zidoune, Mohammed Nasreddine, and Hayaloglu, Ali Adnan

Subjects
CHEESE varieties, GOAT milk, RAW milk, POLYACRYLAMIDE gel electrophoresis, LACTIC acid bacteria, PROTEOLYSIS, DNA, CHEESE
Abstract

Bouhezza is an Algerian traditional cheese made using different types of milk (goat, sheep and cow), ripened in a goat-skin or sheep-skin bag called Chekoua or Djeld of Bouhezza. The objective of the study was the characterization of Bouhezza cheese through ten cheese preparation trials using goat raw milk. The chemical and microbiological composition and proteolysis were monitored on ripened samples. The physicochemical characteristics showed that Bouhezza is acidic with a pH value of 3.95 and 2.36% for titratable acidity as lactic acid, 13.20% for protein and 12.74% for fat. At the end of ripening, Bouhezza was classified to be a ripened, soft and mid-fat cheese. Sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS–PAGE) of Bouhezza samples showed low proteolysis after 30 days of ripening. Microbiological results showed a high content of lactic acid bacteria (LAB), 8 to 9 log cfu/ g, an absence of pathogenic bacteria, and a low level of contamination flora. This makes the cheese a healthy product and of an acceptable hygienic quality. Four proteolytic lactic acid bacteria were identified by 16S ribosomal deoxyribonucleic acid (rDNA) sequencing: two strains of Enterococcus faecalis, one E. faecium, and one Lactobacillus paracasei ssp. paracasei. Reversed phase-high performance liquid chromatography (RP–HPLC) of the soluble fraction at pH 4.4 showed changes occurred during ripening. This work highlights, characterizes, and improves the knowledge of cheese Bouhezza made with raw goat's milk. This product is rich in nutrients, such as proteins and minerals, that are useful to the consumer. [ABSTRACT FROM AUTHOR]

Published
2020
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36. Role of the bolus degree of structure on the protein digestibility during in vitro digestion of a pea protein‐fortified sponge cake chewed by elderly.

Author

Assad‐Bustillos, Melissa, Palier, Juliette, Rabesona, Hanitra, Choiset, Yvan, Della Valle, Guy, and Feron, Gilles

Subjects
PEAS, PROTEIN structure, BOLUS (Digestion), POLYACRYLAMIDE gel electrophoresis, DIGESTION, AMINO group
Abstract

This study investigated the digestibility of proteins in a pea protein‐fortified sponge cake, as well as the impact of the degree of structure of the bolus produced by elderly subjects on the digestibility of proteins by combining ex vivo and in vitro approaches via the standardized protocol INFOGEST. The sponge cakes were consumed by a group of 20 elderly subjects with contrasting physiology, their boli were recovered just before swallowing, and their apparent viscosity was measured to delineate the bolus degree of structure. According to this criterion, two pools were formed with boli from subjects selected at the extremes: low viscosity and high viscosity, with apparent viscosity values (at 120 s−1) of 124 ± 18 and 208 ± 19 Pa s, respectively. The sponge cakes and the two pools underwent in vitro digestion. Protein hydrolysis kinetics was followed by measuring the released primary amino groups (NH2) and by sodium‐dodecyl‐sulfate polyacrylamide gel electrophoresis at different time points. For all samples, the representative bands of pea proteins disappear gradually during digestion, accompanied by the appearance of bands indicating the presence of proteins with MW < 15 kDa. In addition, the NH2 concentrations increase over time and do not differ between sponge cake and pea protein isolate. Moreover, the degree of structure of the food bolus has no significant effect on the concentration of NH2 released. These results showed that pea proteins in a fortified sponge cake are bioaccessible under standardized conditions and that the degree of structure of the bolus did not influence protein digestibility for these foods. [ABSTRACT FROM AUTHOR]

Published
2020
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39. Camel's milk: A new source of proteins for children with cow's milk allergy?

Author

Boughellout, H., Choiset, Yvan, Rabesona, H., Chobert, Jean-Marc, Haertlé, Thomas, Zidoune, M. N., Équipe Transformation et Elaboration des Produits Agro-Alimentaires (TEPA), Laboratoire de Nutrition et Technologies Alimentaires (LNTA), Université Mentouri Constantine [Algérie] (UMC), Institut de la Nutrition de l'Alimentation et des Technologies Agro-Alimentaire (INATAA), Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA), Institut National de la Recherche Agronomique (INRA), and UMR1268, Biopolymères, Interactions Assemblages (BIA)

Subjects
Camel's milk, endocrine system, fluids and secretions, Immunoreactivity, Indirect Elisa, [SDV]Life Sciences [q-bio], food and beverages, Milk proteins, IGE, Cow's milk allergy
Abstract

Introduction. Camel's milk proteins have very little homology with cow's Milk proteins, and, in addition, beta-lactoglobulin, the major allergenic protein in cow's milk, is completely absent in camel's milk. Such structural differences may result in different antigenic responses induced by these two milks. In the present work we studied the immunoreactivity of camel's milk proteins using sera from children with confirmed allergy to cow's milk proteins. Methods. We used milk caseins and whey proteins from Targui camels from Southern Algeria and sera from 10 patients allergic to cow's milk proteins confirmed by their clinical history and by skin tests. The immunoreactivity of camel's and cow's milk proteins was studied by indirect Elisa using these sera. Results. All the 10 sera showed reactivity with cow's milk caseins whereas only 4 of them reacted with camel's milk caseins, and these responses were significantly lower (16 to 92%) compared to the responses to cow's milk proteins. In contrast, all of the whey proteins reacted with the patients' sera, but these responses were lower than those with bovine whey proteins (36 to 85% lower). Discussion. Camel's milk proteins appear to have a very weak antigenic potential in comparison to cow's milk proteins, as has been reported in other studies (Restani et al., 2002; Vereda, 2006; El-Agamy et al., 2007; Fiocchi et al., 2010). Conclusion. The use of camel's milk as a substitute for cow's milk carries a certain risk due to its residual immunoreactivity. Nevertheless, due to its low allergenic potential, it could be considered to be used as a substitute for cow's milk for children at risk of developing cow's milk allergy.

Published
2016
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40. Selection of Lactic Acid Bacteria Isolated from Thai Traditional Fermented Foods to use as Starter Cultures Based on Antioxidant Activity and no Histidine Production.

Author

Usa Panritdam, Duangporn Kantachote, Haertlé, Thomas, Choiset, Yvan, and Rabesona, Hanitra

Subjects
LACTIC acid bacteria, FERMENTED foods, ANTIOXIDANTS, SULFONIC acids, AMINO acids, LACTOBACILLUS
Abstract

Four strains of lactic acid bacteria (LAB), isolated from various Thai traditional fermented foods, were investigated on free radical scavenging activity of 2, 2-diphenyl-1-picrylhydrazyl (DPPH) and 2, 2-Azino-bis-3- ethylbenzothiazoline-6-sulfonic Acid (ABTS). Antioxidant activity by all isolated LAB in intracellular cell free ex- tracts (ICFE) was higher than in intact cells. The LAB strains FF and FB, isolated from fermented foods (fish and sliced beef), their (ICFE) showed the highest radical- scavenging activity for DPPH and ABTS at 65% and 60%, respectively for the former strain. The detection of amino acid decarboxylase of LAB were investigated by growing on decarboxylase medium and quantitatively evaluated by confirmation of amine forming capacity using an HPLC procedure. In this work, all tested LAB strains were tyramine producer; however, the weakest strain was FF followed by strain FB. In contrast, all of them did not produce histamine. Based on 16S rRNA genes, strain FF was identified as Lactobacillus fermentum, while strain FB was Lactobacillus plantarum. Both are potential starter cultures for pro- ducing fermented meat sausages. [ABSTRACT FROM AUTHOR]

Published
2019
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42. Modification of IgE binding to beta- and alpha(S1)-caseins by proteolytic activity of Lactobacillus helveticus A75

Author

Ahmadova Fehruz, Aynur, El-Ghaish, Shady, Choiset, Yvan, Rabesona, Hanitra, Drouet, Martine, Chobert, Jean-Marc, Kuliev, Akif A., Haertlé, Thomas, Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA), Institut National de la Recherche Agronomique (INRA), Baku State University, Unite Allergol Gen & Pneumol, Centre Hospitalier Universitaire d'Angers (CHU Angers), PRES Université Nantes Angers Le Mans (UNAM)-PRES Université Nantes Angers Le Mans (UNAM), NATO project [982164], French Ministry of Foreign Affairs and Education and Embassy of French Republic in Azerbaijan (Service d'Action Culturelle et Scientifique de l'Ambassade de France a Bakou), and Egyptian Ministry of Foreign Affairs and Education

Subjects
[SDV.IDA]Life Sciences [q-bio]/Food engineering, food and beverages, [SPI.GPROC]Engineering Sciences [physics]/Chemical and Process Engineering
Abstract

Proteolytic activity of Lactobacillus helveticus A75 and effects of caseins hydrolysis by this strain on their immuno-reactivity were studied. Proteases of L. helveticus A75 hydrolyzed both alpha(S1)- and beta-caseins and were inhibited by serine-and metalloproteases inhibitors. Polymerase chain reaction amplification revealed the presence of prtH gene, which was 99% identical to prtH gene of L. helveticus CNRZ 32. Effect of proteolysis of alpha(S1)- and beta-caseins by L. helveticus A75 on their immunoglobulin E (IgE) binding ability was studied by an enzyme-linked immunosorbent assay with the pool of eight sera from cow milk allergy patients. The IgE binding ability of hydrolyzed proteins was lower than that of intact proteins, which indicates that hydrolysis of alpha(S1)- and beta-caseins by proteases of L. helveticus A75 decreases their recognition by specific IgE. Half maximal inhibitory concentration values were 2.01 and 2.28 mu g/mL for alpha(S1)- and beta-casein, respectively, and increased until 9.08 and 13.65 mu g/mL, respectively, after their hydrolysis by L. helveticus A75.

Published
2013
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43. Antimicrobial activity, probiotic properties and safety of wild strain Enterococcus faecium AQ71 isolated from Azerbaijani Motal cheese

Author

Ahmadova, Aynur, Todorovc, Svetoslav Dimitrov, Choiset, Yvan, Rabesona, Hanitra, Zadi, Tannaz M., Kuliyevb, Akif, Franco, Bernadette D.G.M., Chobert, Jean-Marc, Haertlé, Thomas, Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA), Institut National de la Recherche Agronomique (INRA), Baku State University, Universidade de São Paulo (USP), and Istanbul Technical University. Istanbul, TUR.

Subjects
Cheese, Enterocins, Probiotics, Enterococcus faecium, Safety, [SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology, [SDV.AEN]Life Sciences [q-bio]/Food and Nutrition
Published
2012

44. Antifungal properties of synthetic fragments and entire durancins isolated from Enterococcus durans A5-11

Author

Belguesmia, Yanath, Choiset, Yvan, Rabesona, Hanitra, Baudy-Floc'h, Michèle, Le Blay, Gwenaëlle, Haertlé, Thomas, Chobert, Jean-Marc, Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA), Institut National de la Recherche Agronomique (INRA), Centre National de la Recherche Scientifique (CNRS), Laboratoire Universitaire de Biodiversité et Ecologie Microbienne (LUBEM), Université de Brest (UBO), ANR-09-ALIA-05 FUNGINIB, and French Antimicrobial Peptides Society (FAPS). Montpellier, FRA. Université des Sciences et Technologies (Lille 1) (USTL).

Subjects
métabolisme des bactéries, Bactériologie, propriété antifongique, bactérie lactique, Bacteriology, Lactic acid bacteria, Enterococcus durans, bacteriocin, antifungal, synthetic peptides, [SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology, peptide, Alimentation et Nutrition, fusarium graminearum, Food and Nutrition, propriété antibactérienne, [SDV.AEN]Life Sciences [q-bio]/Food and Nutrition, entérococcine, ComputingMilieux_MISCELLANEOUS
Abstract

National audience

Published
2012

45. Interlocking of vitamin A in beta-lactoglobulin aggregates produced under high pressure

Author

Mensi, Azza, Choiset, Yvan, de Lamballerie, Marie, Borel, Patrick, Haertlé, Thomas, Chobert, Jean-Marc, Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA), Institut National de la Recherche Agronomique (INRA), Centre National de la Recherche Scientifique (CNRS), Nutrition, obésité et risque thrombotique (NORT), Institut National de la Recherche Agronomique (INRA)-Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM), DECHEMA (DECHEMA). Francfort, DEU. Institut National de la Recherche Agronomique (INRA)., and ProdInra, Migration

Subjects
[SDV.AEN] Life Sciences [q-bio]/Food and Nutrition, [SDV.IDA]Life Sciences [q-bio]/Food engineering, [SDV.IDA] Life Sciences [q-bio]/Food engineering, [SDV.AEN]Life Sciences [q-bio]/Food and Nutrition, ComputingMilieux_MISCELLANEOUS
Abstract

International audience

Published
2012

46. Interactions of β-Lactoglobulin Variants A and B with Vitamin A. Competitive Binding of Retinoids and Carotenoids

Author

Mensi, Azza, Choiset, Yvan, Rabesona, Hanitra, Haertlé, Thomas, Borel, Patrick, and Chobert, Jean-Marc

Abstract

β-Lactoglobulin (β-Lg) is the major whey protein of bovine milk present at a concentration of 2–3 g L–1. Its biological role is still not well-known. However, many studies have suggested that β-Lg may play either nutritional or specific transporter role. The high affinity of β-Lg for retinol and other retinoids was reported. The results of interaction studies of β-Lg with carotenoids, that is, β-carotene, β-cryptoxanthin, and α-carotene, which display similar structures are reported in this study. The affinities of β-Lg for binding of retinoids and carotenoids were compared, providing more information about the binding site(s) of these molecules by β-Lg. Interactions were followed by the measurements of quenching of β-Lg tryptophan fluorescence and retinol fluorescence. The obtained results indicate that carotenoids are bound by β-Lg with high affinity of the order of 10–8M. Measurement of retinol competition with carotenoids for binding by β-Lg suggests that the binding of these two ligands occurs at two different sites of β-Lg.

Published
2024
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47. Conformational dynamics and oligomerization pathways of prion protein investigated by rational mutagenesis

Author

Rezaei, Human, Eghiaian, Frédéric, Daubenfeld, Thorsten, Quenet, Yann, Choiset, Yvan, Haertlé, Thomas, Grosclaude, Jeanne, Unité de recherche Virologie et Immunologie Moléculaires (VIM (UR 0892)), Institut National de la Recherche Agronomique (INRA), Laboratoire des mécanismes réactionnels (DCMR), École polytechnique (X)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), and ProdInra, Migration

Subjects
[SDV] Life Sciences [q-bio], [SDV]Life Sciences [q-bio], ComputingMilieux_MISCELLANEOUS
Abstract

International audience

Published
2005

48. Peptic hydrolysis of ovine beta-lactoglobulin, alpha-lactalbumin. Exceptional susceptibility of native ovine beta-lactoglobulin to pepsinolysis

Author

El-Zahar, K., Sitohy, Mahmoud Zaki, Choiset, Yvan, Métro, François, Haertlé, Thomas, Chobert, J.M., Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA), Institut National de la Recherche Agronomique (INRA), and ProdInra, Migration

Subjects
[SDV.SA]Life Sciences [q-bio]/Agricultural sciences, [SDV.SA] Life Sciences [q-bio]/Agricultural sciences
Published
2005

49. Activité inhibitrice de l'enzyme de conversion de l'angiotensine I(ECA) de peptides trypsiques de la beta-lactoglobuline du lait de brebis et de yoghourts obtenus à partir de différents levains

Author

Chobert, J.M., El-Zahar, K., Sitohy, Mahmoud Zaki, Dalgalarrondo, Michèle, Métro, François, Choiset, Yvan, Haertlé, Thomas, Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA), Institut National de la Recherche Agronomique (INRA), and ProdInra, Migration

Subjects
[SDV.SA]Life Sciences [q-bio]/Agricultural sciences, [SDV.SA] Life Sciences [q-bio]/Agricultural sciences
Published
2005

50. Angiotensin I-converting-enzyme (ACE)-inhibitory activity of tryptic peptides of ovine $\beta$-lactoglobulin and of milk yoghurts obtained by using different starters

Author

Chobert, Jean-Marc, El-Zahar, Khaled, Sitohy, Mahmoud, Dalgalarrondo, Michèle, Métro, François, Choiset, Yvan, Haertlé, Thomas, and Revues Inra, Import

Subjects
[SDV.AEN] Life Sciences [q-bio]/Food and Nutrition, ACE-inhibitory activity---lait de brebis, yaourt, tryptic peptide, activité inhibitrice de l'ECA, peptide trypsique, [SDV.IDA] Life Sciences [q-bio]/Food engineering, ovine milk, yoghurt
Abstract

The aim of this study was to investigate the angiotensin I-converting-enzyme (ACE)-inhibitory activity of tryptic hydrolysates of ovine $\beta$-lactoglobulin, and of yoghurts made by using different starters. Ovine $\beta$-lactoglobulin (a mixture of variants A and B at a ratio of 50/50) was subjected to trypsin activity. The degree of hydrolysis of native whole $\beta$-lactoglobulin reached 56, 72, 93 and 95% after 1, 2, 8 and 24 h, respectively. ACE-inhibitory activity of tryptic hydrolysates increased with the time of hydrolysis, yielding 85, 88 and 92% after 2, 12 and 24 h, respectively. The determination of ACE-inhibitory activity of some tryptic peptides separated by RP-HPLC and identified by mass spectroscopy showed that the more hydrophilic peptides showed the higher activity. Yoghurts obtained by fermentation of ovine milk with four different sets of starters, and their fractions soluble or not at pH 4.6 also showed an ACE-inhibitory activity. The maximum activity was obtained in the case of insoluble fractions at pH 4.6 of yoghurts made with the set of starters YC-183., Activité inhibitrice de l'enzyme de conversion de l'angiotensine I (ECA) de peptides trypsiques de la$\beta$-lactoglobuline du lait de brebis et de yoghourts obtenus à partir de différents levains. Une activité inhibitrice de l'enzyme de conversion de l'angiotensine I (ECA) a été recherchée dans les peptides trypsiques de la $\beta$-lactoglobuline du lait de brebis et dans des fractions issues de yoghourts fabriqués à partir de différents ferments lactiques. La $\beta$-lactoglobuline ovine (un mélange des variants A et B) a été soumise à une hydrolyse trypsique. Les degrés d'hydrolyse de la $\beta$-lactoglobuline ont atteint 56, 72, 93 et 95 % respectivement après 1, 2, 8 et 24 h d'hydrolyse. L'activité inhibitrice de l'ECA des hydrolysats trypsiques augmentait avec la durée de l'hydrolyse, atteignant 85, 88 et 92 % respectivement après 2, 12 et 24 h. La détermination de l'activité inhibitrice de l'ECA de quelques peptides trypsiques séparés par CLHP en phase inversée et identifiés par spectrométrie de masse a montré que les peptides les plus hydrophiles présentaient l'activité la plus grande. Des yoghourts fabriqués par fermentation du lait de brebis à l'aide de quatre compositions différentes de levains ainsi que leurs fractions solubles ou non à pH 4,6 présentaient aussi une activité inhibitrice de l'ECA. Le maximum d'activité a été obtenu avec les fractions insolubles à pH 4,6 de yoghourts fabriqués avec le levain YC-183.

Published
2005

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