Abstract

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.

Keywords

Potato protein; Nanomaterials; Biobased materials; Amyloid; Mass spectrometry

Published in

ACS Sustainable Chemistry and Engineering
2020, Volume: 8, number: 2, pages: 1058-1067
Publisher: AMER CHEMICAL SOC

SLU Authors

• Langton, Maud

  • Department of Molecular Sciences, Swedish University of Agricultural Sciences
    

Sustainable Development Goals

SDG2 End hunger, achieve food security and improved nutrition and promote sustainable agriculture


UKÄ Subject classification

Plant Biotechnology
Biochemistry and Molecular Biology


Publication identifier

DOI: https://doi.org/10.1021/acssuschemeng.9b05865

Permanent link to this page (URI)

https://res.slu.se/id/publ/104346