Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Jean-Luc Mession"'
Publikováno v:
Food Hydrocolloids. 73:344-357
In our preceding study (Part I), the thermal denaturation and aggregation of enriched pea protein fractions, namely vicilin/convicilin 7S (Vic) and legumin 11S (Leg), were investigated in the absence or in presence of casein micelles (CM) at pH ≈ 7
Autor:
Karima Laleg, Florence Husson, Valerie Micard, Yves Boirie, Christophe Giraudet, Insaf Berrazaga, Jean-Luc Mession, O. Le Bacquer, Christelle Guillet, Rémi Saurel, Véronique Patrac, Jérôme Salles, Stéphane Walrand
Publikováno v:
Journal of Dairy Science
Journal of Dairy Science, American Dairy Science Association, 2019, 102 (2), pp.1066-1082. ⟨10.3168/jds.2018-14610⟩
Journal of Dairy Science, 2019, 102 (2), pp.1066-1082. ⟨10.3168/jds.2018-14610⟩
Journal of Dairy Science, American Dairy Science Association, 2019, 102 (2), pp.1066-1082. ⟨10.3168/jds.2018-14610⟩
Journal of Dairy Science, 2019, 102 (2), pp.1066-1082. ⟨10.3168/jds.2018-14610⟩
International audience; Food formulation and process conditions can indirectly influence AA digestibility and bioavailability. Here we investigated the effects of formulation and process conditions used in the manufacture of novel blended dairy gels
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b185667abfea0a35ba591574d5dac0cf
https://hal.archives-ouvertes.fr/hal-02382900
https://hal.archives-ouvertes.fr/hal-02382900
Publikováno v:
Food Hydrocolloids. 46:233-243
This report focuses on cold-set gelation of pea ( Pisum sativum L.) proteins and related globulin fractions, namely Vicilin 7S and Legumin 11S. Protein thermal denaturation and aggregation were investigated using differential scanning calorimetry (DS
Publikováno v:
Food Hydrocolloids
Food Hydrocolloids, Elsevier, 2017, 67, pp.229-242. 〈10.1016/j.foodhyd.2015.12.015〉
Food Hydrocolloids, Elsevier, 2017, 67, pp.229-242. ⟨10.1016/j.foodhyd.2015.12.015⟩
Food Hydrocolloids, Elsevier, 2017, 67, pp.229-242. 〈10.1016/j.foodhyd.2015.12.015〉
Food Hydrocolloids, Elsevier, 2017, 67, pp.229-242. ⟨10.1016/j.foodhyd.2015.12.015⟩
International audience; The aim of this work was to investigate the heat-induced interactions between pea proteins (vicilin 7S or legumin 11S enriched-fractions) in admixture with suspended casein micelles (SCM), at weight protein ratio of 1:1 and pH
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f45c7085f42fce00142aa93c8e9fd8c8
https://hal-univ-bourgogne.archives-ouvertes.fr/hal-01533202
https://hal-univ-bourgogne.archives-ouvertes.fr/hal-01533202
Autor:
Christophe Giraudet, Valérie Micard, Karima Laleg, Florence Husson, Jean-Luc Mession, Insaf Berrazaga, Christelle Guillet, Stéphane Walrand, Yves Boirie, Rémi Saurel, O. Le Bacquer, Jérôme Salles, Véronique Patrac
Publikováno v:
Nutrition Clinique et Métabolisme. 32:249-250
Introduction et but de l’etude L’impact environnemental et les risques pour la sante associes a la production et la consommation excessive de sources de proteines animales pourraient etre limites par l’augmentation de la part des proteines vege
Autor:
Ali Assifaoui, Rémi Saurel, Coralie Blanchard, Céline Lafarge, Jean-Luc Mession, Fatma-Vall Mint-Dah
Publikováno v:
Food Hydrocolloids. 31:446-457
A multi-scale investigation of pea proteins – alginate cold-set gels was proposed in this study. The gel preparation followed a two-steps procedure. Globular pea proteins were first denatured and aggregated by a pre-heating step. Sodium alginate wa
Publikováno v:
Journal of Agricultural and Food Chemistry
Journal of Agricultural and Food Chemistry, American Chemical Society, 2016, 64 (13), pp.2780-2791. ⟨10.1021/acs.jafc.6b00087⟩
Journal of Agricultural and Food Chemistry, American Chemical Society, 2016, 64 (13), pp.2780-2791. 〈10.1021/acs.jafc.6b00087〉
Journal of Agricultural and Food Chemistry, American Chemical Society, 2016, 64 (13), pp.2780-2791. ⟨10.1021/acs.jafc.6b00087⟩
Journal of Agricultural and Food Chemistry, American Chemical Society, 2016, 64 (13), pp.2780-2791. 〈10.1021/acs.jafc.6b00087〉
International audience; The present work investigates the formation of protein aggregates (85 degrees C, 60 min incubation) upon heat treatment of beta-lactoglobulin (beta lg) pea globulins (Glob) mixtures at pH 7.2 and 5 mM NaCl from laboratory-prep
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::af1bfc980f592cbdcd88a409dd1aae2f
https://hal-univ-bourgogne.archives-ouvertes.fr/hal-01484271
https://hal-univ-bourgogne.archives-ouvertes.fr/hal-01484271
Publikováno v:
Food Hydrocolloids. 29:335-346
Soluble and natural mixed pea proteins (PP) were extracted from defatted pea seeds according to acidic precipitation (PPP) or ultrafiltration/diafiltration (PPDF) procedures. The isolates contained proteins with a low level of denaturation. Mixed pea
Publikováno v:
Food Hydrocolloids. 28:333-343
The physicochemical properties of a native, globular plant protein–linear anionic polysaccharide aqueous system at 20 °C were investigated in conditions where biopolymers carry a net negative charge (pH 7.2, 0.1 M NaCl). The pea proteins–sodium
Publikováno v:
Food Chemistry
Food Chemistry, Elsevier, 2014, 164, pp.406-412. ⟨10.1016/j.foodchem.2014.05.008⟩
Food Chemistry, Elsevier, 2014, 164, pp.406-412. ⟨10.1016/j.foodchem.2014.05.008⟩
International audience; This study is based on the assumption that the off-flavour of pea proteins might be decreased using the retention of volatile compounds by a mixture with another biopolymer. The partition of volatile compounds in an aqueous sy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5f4493cfdc766762c6b2dd86397854b5
https://hal-agrosup-dijon.archives-ouvertes.fr/hal-03006674
https://hal-agrosup-dijon.archives-ouvertes.fr/hal-03006674