Title :

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

Author(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

Journal title :

International Dairy Journal

Volume number :

143

Pages :

105688

Publisher :

Elsevier BV

Publication date :

2023-08

ISSN :

0958-6946

HAL domain(s) :

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

English abstract : [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 ...
Show more >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.Show less >

Language :

Anglais

Peer reviewed article :

Oui

Audience :

Internationale

Popular science :

Non

Administrative institution(s) :

Université de Lille
CNRS
INRAE
ENSCL

Collections :

• Unité Matériaux et Transformations (UMET) - UMR 8207

Research team(s) :

Processus aux Interfaces et Hygiène des Matériaux (PIHM)

Submission date :

2024-02-08T14:43:04Z