The assembly mechanism and mesoscale architecture of protein–polysaccharide complexes formed at the solid–liquid Interface

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dc.contributor.authorBiswas, Sen_AU
dc.contributor.authorMelton, LDen_AU
dc.contributor.authorNelson, ARJen_AU
dc.contributor.authorLe Brun, APen_AU
dc.contributor.authorHeinrich, Fen_AU
dc.contributor.authorMcGillivray, DJen_AU
dc.contributor.authorXu, AYen_AU
dc.date.accessioned2024-08-26T02:57:45Zen_AU
dc.date.available2024-08-26T02:57:45Zen_AU
dc.date.issued2022-10-04en_AU
dc.date.statistics2024-08en_AU
dc.description.abstractProtein-polysaccharide composite materials have generated much interest due to their potential use in medical science and biotechnology. A comprehensive understanding of the assembly mechanism and the mesoscale architecture is needed for fabricating protein-polysaccharide composite materials with desired properties. In this study, complex assemblies were built on silica surfaces through a layer-by-layer (LbL) approach using bovine beta-lactoglobulin variant A (βLgA) and pectin as model protein and polysaccharide, respectively. We demonstrated the combined use of quartz crystal microbalance with dissipation monitoring (QCM-D) and neutron reflectometry (NR) for elucidating the assembly mechanism as well as the internal architecture of the protein-polysaccharide complexes formed at the solid-liquid interface. Our results show that βLgA and pectin interacted with each other and formed a cohesive matrix structure at the interface consisting of intertwined pectin chains that were cross-linked by βLgA-rich domains. Although the complexes were fabricated in an LbL fashion, the complexes appeared to be relatively homogeneous with βLgA and pectin molecules spatially distributed within the matrix structure. Our results also demonstrate that the density of βLgA-pectin complex assemblies increased with both the overall and local charge density of pectin molecules. Therefore, the physical properties of the protein-polysaccharide matrix structure, including density and level of hydration, can be tuned by using polysaccharides with varying charge patterns, thus promoting the development of composite materials with desired properties. © 2024 American Chemical Societyen_AU
dc.description.sponsorshipThis work is supported by Bioprocessing and Bioengineering Grant No. 2022-67022-38145 from the USDA National Institute of Food and Agriculture. A.Y.X. also acknowledges the financial support from the National Science Foundation EPSCoR-Louisiana Materials Design Alliance (LAMDA) program (Grant No. OIA-1946231). The authors would also like to thank the Australian Institute of Nuclear Science and Engineering (AINSE Limited) for providing travel support to ANSTO for neutron experiments. ANSTO is thanked for the provision of beamtime. Prof. Jenny Malmstrom from the University of Auckland and Prof. Bill Williams from Massey University are acknowledged for valuable discussions.en_AU
dc.format.mediumPrint-Electronicen_AU
dc.identifier.citationBiswas, S., Melton, L. D., Nelson, A. R. J., Le Brun, A. P., Heinrich, F., McGillivray, D. J., & Xu, A. Y. (2022). The assembly mechanism and mesoscale architecture of protein–polysaccharide complexes formed at the solid–liquid Interface. Langmuir, 38(41), 12551-12561. doi:10.1021/acs.langmuir.2c02003en_AU
dc.identifier.issn0743-7463en_AU
dc.identifier.issn1520-5827en_AU
dc.identifier.issue41en_AU
dc.identifier.journaltitleLangmuiren_AU
dc.identifier.pagination12551-12561en_AU
dc.identifier.urihttp://dx.doi.org/10.1021/acs.langmuir.2c02003en_AU
dc.identifier.urihttps://apo.ansto.gov.au/handle/10238/15671en_AU
dc.identifier.volume38en_AU
dc.languageEnglishen_AU
dc.language.isoenen_AU
dc.publisherAmerican Chemical Societyen_AU
dc.subjectCarbohydratesen_AU
dc.subjectLayersen_AU
dc.subjectMoleculesen_AU
dc.subjectProtein structureen_AU
dc.subjectSilicaen_AU
dc.subjectPolysaccharidesen_AU
dc.subjectNeutron reflectorsen_AU
dc.subjectPectinsen_AU
dc.titleThe assembly mechanism and mesoscale architecture of protein–polysaccharide complexes formed at the solid–liquid Interfaceen_AU
dc.typeJournal Articleen_AU
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