| Autor: |
Mikkel Madsen, Sanaullah Khan, Sonja Kunstmann, Finn L. Aachmann, Richard Ipsen, Peter Westh, Cecilia Emanuelsson, Birte Svensson |
| Jazyk: |
angličtina |
| Rok vydání: |
2022 |
| Předmět: |
|
| Zdroj: |
Food Chemistry: Molecular Sciences, Vol 5, Iss , Pp 100137- (2022) |
| Druh dokumentu: |
article |
| ISSN: |
2666-5662 |
| DOI: |
10.1016/j.fochms.2022.100137 |
| Popis: |
There is a dogma within whey protein modification, which dictates the necessity of pretreatment to enzymatic cross-linking of β-lactoglobulin (β-Lg). Here microbial transglutaminase (MTG) cross-linked whey proteins and β-Lg effectively in 50 mM NaHCO3, pH 8.5, without pretreatment. Cross-linked β-Lg spanned 18 to >240 kDa, where 6 of 9 glutamines reacted with 8 of 15 lysines. The initial isopeptide bond formation caused loss of β-Lg native structure with t1/2 = 3 h, while the polymerization occurred with t1/2 = 10 h. Further, cross-linking effects on protein carbohydrate interaction have been overlooked, leaving a gap in understanding of these complex food matrices. Complexation with alginate showed that β-Lg cross-linking decreased onset of particle formation, hydrodynamic diameter, stoichiometry (β-Lg/alginate) and dissociation constant. The complexation was favored at higher temperatures (40 °C), suggesting that hydrophobic interactions were important. Thus, β-Lg was cross-linked without pretreatment and the resulting polymers gave rise to altered complexation with alginate. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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