Unaided efficient transglutaminase cross-linking of whey proteins strongly impacts the formation and structure of protein alginate particles
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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.
| Originalsprog | Engelsk |
|---|---|
| Artikelnummer | 100137 |
| Tidsskrift | Food Chemistry: Molecular Sciences |
| Vol/bind | 5 |
| Antal sider | 11 |
| DOI | |
| Status | Udgivet - 2022 |
Bibliografisk note
Funding Information:
Karina Jansen (DTU Bioengineering) is gratefully acknowledged for technical support and Assist. Prof. Gael Clergeaud Veiga (DTU Health Tech) for DLS analyses. Science manager Jeppe W. Tams (Novozymes) is thanked for the MTG, seaweed R&D Leader Trond Helgerud (DuPont Nutrition and Bioscience) for AlgM, and Senior Innovation Manager Jacob Holm Nielsen (Arla Foods Ingredients) for SPC. We thank Prof. Jens Preben Morth for use of the fluorimeter and circular dichroism spectrometer and Prof. Alexander Büll and Dr. Emil G.P. Stender for introduction and use of ProbeDrum. All mass spectrometry was performed at DTU Proteomics Core with help and guidance of Lene H. Blicher and Assoc. Prof. Erwin M. Schoof. The work is supported by the Novo Nordisk Foundation (NNF), Denmark Biotechnology Synthesis and Production (grant NNFOC0027616) and a third of a PhD stipend (to MM) from the Technical University of Denmark.
Funding Information:
The work is supported by the Novo Nordisk Foundation (NNF), Denmark Biotechnology Synthesis and Production (grant NNFOC0027616 ) and a third of a PhD stipend (to MM) from the Technical University of Denmark.
Publisher Copyright:
© 2022 The Authors
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