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Legume protein fermented by lactic acid bacteria: Specific enzymatic hydrolysis, protein composition, structure, and functional properties.

Authors :
Du Q
Li H
Tu M
Wu Z
Zhang T
Liu J
Ding Y
Zeng X
Pan D
Source :
Colloids and surfaces. B, Biointerfaces [Colloids Surf B Biointerfaces] 2024 Jun; Vol. 238, pp. 113929. Date of Electronic Publication: 2024 Apr 24.
Publication Year :
2024

Abstract

In recent years, with increasing emphasis on healthy, green, and sustainable consumption concepts, plant-based foods have gained popularity among consumers. As widely sourced plant-based raw materials, legume proteins are considered sustainable and renewable alternatives to animal proteins. However, legume proteins have limited functional properties, which hinder their application in food products. LAB fermentation is a relatively natural processing method that is safer than chemical/physical modification methods and can enrich the functional properties of legume proteins through biodegradation and modification. Therefore, changes in legume protein composition, structure, and functional properties and their related mechanisms during LAB fermentation are described. In addition, the specific enzymatic hydrolysis mechanisms of different LAB proteolytic systems on legume proteins are also focused in this review. The unique proteolytic systems of different LAB induce specific enzymatic hydrolysis of legume proteins, resulting in the production of hydrolysates with diverse functional properties, including solubility, emulsibility, gelability, and foamability, which are determined by the composition (peptide/amino acid) and structure (secondary/tertiary) of legume proteins after LAB fermentation. The correlation between LAB-specific enzymatic hydrolysis, protein composition and structure, and protein functional properties will assist in selecting legume protein raw materials and LAB strains for legume plant-based food products and expand the application of legume proteins in the food industry.<br />Competing Interests: Declaration of Competing Interest The authors have no conflicts of interest to declare.<br /> (Copyright © 2024 Elsevier B.V. All rights reserved.)

Details

Language :
English
ISSN :
1873-4367
Volume :
238
Database :
MEDLINE
Journal :
Colloids and surfaces. B, Biointerfaces
Publication Type :
Academic Journal
Accession number :
38677155
Full Text :
https://doi.org/10.1016/j.colsurfb.2024.113929