2020
DOI: 10.1016/j.foodchem.2020.126301
|View full text |Cite
|
Sign up to set email alerts
|

Transglutaminase modifies the physical stability and digestibility of chickpea protein-stabilized oil-in-water emulsions

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
3
1
1

Citation Types

1
36
0

Year Published

2021
2021
2024
2024

Publication Types

Select...
8
1

Relationship

0
9

Authors

Journals

citations
Cited by 72 publications
(37 citation statements)
references
References 50 publications
1
36
0
Order By: Relevance
“…Usually, the goal of crosslinking is to improve the textural properties of the protein by building up the polypeptides into stronger structures. TG (EC 2.3.2.13) is the only commercially available food‐grade cross‐linking enzyme and it been reported to improve texture, viscosity, ES, gelation, foam and increase hydrophobicity properties of food proteins (Djoullah, Husson, & Saurel, 2018; Glusac, Isaschar‐Ovdat, & Fishman, 2020; Nivala, Mäkinen, Kruus, Nordlund, & Ercili‐Cura, 2017; Sun, & Arntfield, 2011a). Sun & Arntfield (2011a), reported that TG increased the gel strength of PPI 8 times and SPI gel by 2 times in comparison to the gel made from untreated protein; gel strength also increased with higher TG levels.…”
Section: Modification Of Plant Proteins By Various Processing Techniquesmentioning
confidence: 99%
“…Usually, the goal of crosslinking is to improve the textural properties of the protein by building up the polypeptides into stronger structures. TG (EC 2.3.2.13) is the only commercially available food‐grade cross‐linking enzyme and it been reported to improve texture, viscosity, ES, gelation, foam and increase hydrophobicity properties of food proteins (Djoullah, Husson, & Saurel, 2018; Glusac, Isaschar‐Ovdat, & Fishman, 2020; Nivala, Mäkinen, Kruus, Nordlund, & Ercili‐Cura, 2017; Sun, & Arntfield, 2011a). Sun & Arntfield (2011a), reported that TG increased the gel strength of PPI 8 times and SPI gel by 2 times in comparison to the gel made from untreated protein; gel strength also increased with higher TG levels.…”
Section: Modification Of Plant Proteins By Various Processing Techniquesmentioning
confidence: 99%
“…Proteins from legumes have been gaining traction as a necessity more than a choice due to their high nutritional benefits, hypo-allergenicity, gluten-free and non-genetically modified organism labels, affordability, high productivity and versatility Boukid et al, 2019). Proteins from legumes also exhibit a wide range of techno-and bio-functional applications comparable with proteins from animal and dairy sources providing a multitude of health benefits (Sharif et al, 2018;Boukid et al, 2019;Glusac et al, 2020). The industry of proteins from legumes keep expanding beyond pea to lupine, mung, faba and chickpea proteins (Research & Markets, 2018;Boukid et al, 2019).…”
Section: Introductionmentioning
confidence: 99%
“…Several studies have reported biological activities in chickpea proteins including antioxidant activity, antifungal activity, antigenic activity and metal-chelating ability (Kou et al, 2013;Ghribi et al, 2015c). Chickpea protein is, therefore, a promising health-beneficial ingredient for new products development (Glusac et al, 2020;Xing et al, 2020).…”
Section: Introductionmentioning
confidence: 99%
“…Cross-linking with transglutaminase is generally applied to legume proteins for improving gelling properties. However, Glusac et al [47] studied its effects on characteristics of emulsions stabilized by chickpea protein. Cross-linking treatment was reported to increase mean droplet size of the emulsion compared to the native protein and formed a gel-like structure.…”
Section: Cross-linkingmentioning
confidence: 99%