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Conference papers

Ovalbumin aggregation due to heating in solution increases its in vitro digestibility, compared to the native and dry-heated protein

Catherine Guérin-Dubiard 1 N. Musikaphun Didier Dupont Julien Jardin V. Briard-Bion M. Pasco Francoise Nau 1
1 STLO - Science et Technologie du Lait et de l'Oeuf
Abstract : Ovalbumin aggregation due to heating in solution increases its in vitro digestibility, compared to the native and dry-heated protein
keyword : Ovalbumine agregation digestion protéine native in vitro
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Conference papers
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https://hal-agrocampus-ouest.archives-ouvertes.fr/hal-00849243
Contributor : Céline Martel Connect in order to contact the contributor
Submitted on : Tuesday, July 30, 2013 - 2:55:31 PM
Last modification on : Wednesday, April 6, 2022 - 4:08:11 PM

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  • HAL Id : hal-00849243, version 1

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AGROCAMPUS-OUEST | UNAM | INRA | AGROCAMPUS-OUEST-UMR-STLO | INRAE | STLO

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Catherine Guérin-Dubiard, N. Musikaphun, Didier Dupont, Julien Jardin, V. Briard-Bion, et al.. Ovalbumin aggregation due to heating in solution increases its in vitro digestibility, compared to the native and dry-heated protein. 1 st Food Structures, Digestion & Health Conference, 2012, Palmerston (NZ), New Zealand. ⟨hal-00849243⟩

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