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

Catherine Guérin-Dubiard; N. Musikaphun; Didier Dupont; Julien Jardin; V. Briard-Bion; M. Pasco; Francoise Nau

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

Document type :

Conference papers

Domain :

Life Sciences [q-bio] / Biochemistry, Molecular Biology

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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

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

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

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