Langton, Maud
- Institutionen för molekylära vetenskaper, Sveriges lantbruksuniversitet
Sammanfattning
Protein nanofibrils have emerged as promising building blocks in functional bio/nanomaterials as well as in food products. We here demonstrate that nanofibrils with amyloid-like properties can be produced from potato protein isolate, a major sidestream from the starch industry. Methods for solubilization of potato proteins are evaluated, and a protocol for the assembly of protein nanofibrils is presented. Characterization of the nanofibrils shows that they are rich in beta-sheet structure and display the cross-beta X-ray fiber diffraction pattern, which is a hallmark of amyloid-like fibrils. Atomic force microscopy shows that the fibrils are ca. 4-5 nm in diameter with a nanoscale morphology that displays a high degree of curvature. Using mass spectrometry we identify four peptides that constitute the core building blocks of the nanofibrils and show that they originate from two different classes of proteins. The structural characteristics of these peptides are distinct from previously studied plant protein nanofibrils and thereby reveal new knowledge about the formation of protein nanostructures from agricultural resources.
Nyckelord
Potato protein; Nanomaterials; Biobased materials; Amyloid; Mass spectrometry
Publicerad i
ACS Sustainable Chemistry and Engineering
2020, volym: 8, nummer: 2, sidor: 1058-1067
Utgivare: AMER CHEMICAL SOC
SLU författare
Globala målen (SDG)
UKÄ forskningsämne
Växtbioteknologi
Molekylärbiologi
Biokemi
Publikationens identifierare
- DOI: https://doi.org/10.1021/acssuschemeng.9b05865
Permanent länk till denna sida (URI)
https://res.slu.se/id/publ/104346