Titre :

Transglutaminase cross-linking on dairy proteins: Functionalities, patents, and commercial uses

Auteur(s) :

Velazquez Dominguez, Angella [Auteur]
Unité Matériaux et Transformations - UMR 8207 [UMET]
Hiolle, Manon [Auteur]
abdallah, marwan [Auteur]
Unité Matériaux et Transformations - UMR 8207 [UMET]
Delaplace, Guillaume [Auteur]
Unité Matériaux et Transformations (UMET) - UMR 8207
Peres De Sa Peixoto Jr, Paulo [Auteur]
Unité Matériaux et Transformations (UMET) - UMR 8207

Titre de la revue :

International Dairy Journal

Numéro :

143

Pagination :

105688

Éditeur :

Elsevier BV

Date de publication :

2023-08

ISSN :

0958-6946

Discipline(s) HAL :

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

Résumé en anglais : [en]

Microbial transglutaminase (mTGase) is a known enzyme capable of modifying the structure of proteins through the formation of cross-linking, resulting in protein polymerisation. Milk proteins are an excellent substrate for ...
Lire la suite >Microbial transglutaminase (mTGase) is a known enzyme capable of modifying the structure of proteins through the formation of cross-linking, resulting in protein polymerisation. Milk proteins are an excellent substrate for mTGase cross-linking. The cross-linking formation is related to the environmental conditions of incubation, including pH, temperature, protein concentration, enzyme concentration, and mineral or reducing agents addition; thus, it is vital to better understand the leverages for the protein cross-linking. To elucidate how these leverages affect the cross-linking reaction, the current state of knowledge concerning the impact of environmental conditions on the enzymatic cross-linking between milk proteins was scouted. The potential applications of mTGase cross-linked dairy proteins on food products such as cross-linked milk powders, protein beverages, processed cheese, ice cream, encapsulation of bioactive compounds, and edible films are described. Additionally, the patents addressing the functionalisation of milk products through enzymatic modification are reported.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 :

2024-02-08T14:43:04Z