2005
DOI: 10.1002/bip.20372
|View full text |Cite
|
Sign up to set email alerts
|

Micellization of casein‐graft‐dextran copolymer prepared through Maillard reaction

Abstract: Casein is almost insoluble at around pH 4.6, which is its isoelectric point (pI). Grafting copolymer, casein-g-dextran, was prepared through the Amadori rearrangement of the Maillard reaction. The copolymer has a reversible pH sensitive property: micellization at the pI of casein forming a casein core and dextran shell structure and dissociation when pH differs from the pI. The micelles produced at pH 4.6 have a spherical shape and their size is dependent on the Maillard reaction: reaction time, molar ratio of… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1
1

Citation Types

4
58
0

Year Published

2006
2006
2022
2022

Publication Types

Select...
5
3

Relationship

1
7

Authors

Journals

citations
Cited by 61 publications
(62 citation statements)
references
References 49 publications
4
58
0
Order By: Relevance
“…These results are in agreement with the value of around pH 5.0, the published isoelectric point [34] and the calculated overall neutrality of β-casein [35]. The very close zero potential pH values of β-casein and β-casein-graft-dextran copolymer imply that the Maillard reaction was controlled in its early stage and aminoketose-the Amadori product was mainly obtained [13,26].…”
Section: Graft Degree Analysis Of β-Casein-graft-dextran Copolymersupporting
confidence: 92%
See 2 more Smart Citations
“…These results are in agreement with the value of around pH 5.0, the published isoelectric point [34] and the calculated overall neutrality of β-casein [35]. The very close zero potential pH values of β-casein and β-casein-graft-dextran copolymer imply that the Maillard reaction was controlled in its early stage and aminoketose-the Amadori product was mainly obtained [13,26].…”
Section: Graft Degree Analysis Of β-Casein-graft-dextran Copolymersupporting
confidence: 92%
“…Casein-graft-dextran 35 kDa with high graft degree (molar ratio of casein to 35 kDa dextran 1:8, 20 h Maillard reaction) was also used to study its emulsifying properties at pH 4.6 and 8.0. The limit of the Maillard reaction time is 20 h for casein [26], and 24 h for β-casein in the condition we used to avoid the side reaction, that is, the graft degree of the high-graft casein and β-casein copolymers used in emulsifying study is the maximum. All the copolymer solutions were prepared freshly to avoid the further aggregation or dissociation as discussed above.…”
Section: Evaluation Of the Emulsifying Activity Of The Copolymersmentioning
confidence: 99%
See 1 more Smart Citation
“…In this context, three main approaches can be applied. The first one is based on the copolymerization of casein with synthetic polymers such as acrylic acid (Zhen, Wang, Xie, Wu, & Jiang, 2013) or dextran (Pan et al, 2006). The second one is based on the formation of nanoparticles via electrostatic complexation between the protein and polysaccharides, including Arabic gum (Ye, Flanagan, & Singh, 2006) or chitosan (Anal, Tobiassen, Flanagan, & Singh, 2008).…”
Section: Discussionmentioning
confidence: 99%
“…Diminutions of the amounts of available lysine directly reflect the modification of e-amino groups of basic amino acids upon a Maillard reaction induced addition of sugar molecules to proteins in initial reaction stages. Thus, lysine and arginine modifications were reported for casein/lactose (Scaloni et al, 2002), casein/dextran (Pan, Mu, Hu, Yao, & Jiang, 2006), caseinate/glucose (Gu et al, 2009;Oliver et al, 2006a), caseinate/lactose (Oliver et al, 2006b), caseinate/pectin (Al-Hakkak & Kavale, 2002), caseinomacropeptide/lactose (Moreno, López-Fandiño, & Olano, 2002), b-lactoglobulin/lactose (Chevalier, Chobert, Mollé, et al, 2001;Fenaille, Morgan, Parisod, Tabet, & Guy, 2004;Morgan, Molle, et al, 1999), total milk protein/lactose (De Block et al, 2003) and whey protein/maltodextrin Maillard products (Akhtar & Dickinson, 2007). A modification degree of lysine of up to 100% was detected post Maillard reaction (60°C, 67% r.h., 48 h) of sodium caseinate/glucose mixtures, of up to 80% post Maillard reaction (60°C, 67% r.h., 24 h) of sodium caseinate/lactose mixtures (Oliver et al, 2006b).…”
Section: Tropho-functional Properties Of Enzymatically Treated Milk Pmentioning
confidence: 90%