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Supramolecular self-assembly strategies of natural-based β-lactoglobulin modulating bitter perception of goat milk–derived bioactive peptides
- Source :
- Journal of Dairy Science, Vol 107, Iss 7, Pp 4174-4188 (2024)
- Publication Year :
- 2024
- Publisher :
- Elsevier, 2024.
-
Abstract
- ABSTRACT: Complete self-assembly and reassembly behavior of bitter peptide-protein necessitates multilevel theories that encompass phenomena ranging from the self-assembly of recombinant complex to atomic trajectories. An extension to the level of mechanism method was put forth, involves limited enzymatic digestion and bottom-up proteomics to dissect inherent heterogeneity within β-LG and β-LG-PPGLPDKY complex and uncover conformational and dynamic alterations occurring in specific local regions of the model protein. Bitter peptide PPGLPDKY spontaneously bound to IIAEKTK, IDALNENK, and YLLFCMENSAEPEQSLACQCLVR regions of β-LG in a 1:1 stoichiometric ratio to mask bitterness perception. Molecular dynamic simulation and free energy calculation provided time-varying atomic trajectories of the recombinant complex and found that a peptide was stabilized in the upper region of the hydrophobic cavity with the binding free energy of −30.56 kJ mol−1 through 4 hydrogen bonds (Glu74, Glu55, Lys69, and Ser116) and hydrophobic interactions (Asn88, Asn90, and Glu112). Current research aims to provide valuable physical insights into the macroscopic self-assembly behavior between proteins and bitter peptides, and the meticulous design of highly acceptable taste characteristics in goat milk products.
Details
- Language :
- English
- ISSN :
- 00220302 and 20232438
- Volume :
- 107
- Issue :
- 7
- Database :
- Directory of Open Access Journals
- Journal :
- Journal of Dairy Science
- Publication Type :
- Academic Journal
- Accession number :
- edsdoj.8af37946397d4de7855aa2a9457387e6
- Document Type :
- article
- Full Text :
- https://doi.org/10.3168/jds.2023-24386