Titre :

Sugar type matters in spray drying II: Glycation effects on physicochemical characteristics of aged lactose-hydrolyzed milk powder

Auteur(s) :

Fialho, Tatiana Lopes [Auteur]
Universidade Federal de Viçosa [Brasil] = Federal University of Viçosa [Brazil] = Université fédérale de Viçosa [Brésil] [UFV [Brésil]]
Nascimento, Luis Gustavo Lima [Auteur]
Universidade Federal de Viçosa [Brasil] = Federal University of Viçosa [Brazil] = Université fédérale de Viçosa [Brésil] [UFV [Brésil]]
Moreau, Anne [Auteur]
Unité Matériaux et Transformations (UMET) - UMR 8207
Delaplace, Guillaume [Auteur]
Unité Matériaux et Transformations (UMET) - UMR 8207
Martins, Evandro [Auteur]
Universidade Federal de Viçosa [Brasil] = Federal University of Viçosa [Brazil] = Université fédérale de Viçosa [Brésil] [UFV [Brésil]]
Tuler Perrone, Ítalo [Auteur]
Universidade Federal de Juiz de Fora [UFJF]
Carvalho, Antônio Fernandes de [Auteur]
Universidade Federal de Viçosa [Brasil] = Federal University of Viçosa [Brazil] = Université fédérale de Viçosa [Brésil] [UFV [Brésil]]
Peres De Sa Peixoto Jr, Paulo [Auteur]
Unité Matériaux et Transformations (UMET) - UMR 8207

Titre de la revue :

Food Structure

Pagination :

100215

Éditeur :

Elsevier BV

Date de publication :

2021-10

ISSN :

2213-3291

Discipline(s) HAL :

Sciences du Vivant [q-bio]/Ingénierie des aliments

Résumé en anglais : [en]

Lactose hydrolyzed milk powder has low stability at high temperatures or humidity levels, which results in storage technological problems. The molecular structure has been evaluated for powders submitted to accelerated ...
Lire la suite >Lactose hydrolyzed milk powder has low stability at high temperatures or humidity levels, which results in storage technological problems. The molecular structure has been evaluated for powders submitted to accelerated aging (60 °C for 8 h and 24 h) to understand how lactose hydrolysis induces these issues over time. The powders have been evaluated for particle morphology, molecular structures, and rehydration time. The data show that accelerates aging, at the molecular scale, first promotes glycation and a partial unfolding of proteins. In a second time, the same treatment does increase the number of protein-protein covalent links, however, the amount of such protein-protein links is relatively small and it does not completely explain the observed solubility decrease. Instead, the present results indicate that the loss in solubility is rather a consequence of protein glycation which promotes molecular disorder and the subsequence formation of non-native interactions between casein micelles.Lire moins >

Langue :

Anglais

Comité de lecture :

Oui

Audience :

Internationale

Vulgarisation :

Non

Établissement(s) :

Université de Lille
CNRS
INRAE
ENSCL

Collections :

• Unité Matériaux et Transformations (UMET) - UMR 8207

Équipe(s) de recherche :

Processus aux Interfaces et Hygiène des Matériaux (PIHM)

Date de dépôt :

2023-12-22T13:23:13Z