Abstract

Artificial amyloid fibrils derived from food proteins have attracted significant interest due to their diverse functionalities in food science, materials engineering, and nanotechnology. As a strategical global biomass resource, Antarctic krill proteins (AKP) were extracted from defatted krill meal and self-assembled into amyloid fibrils (AKAF) under pH 2.0 and elevated temperature. The mesoscopic properties of AKAF were characterized using soft matter physics approaches. Results showed that mature AKAF exhibit an average height of 1.8 nm and a contour length of 1.8 μm, featuring a periodic helical structure with a pitch of 25.0 nm. Additionally, AKAF display remarkable mechanical rigidity with a persistence length of 5.9 μm and Young’s modulus of ∼15.5 GPa, exceeding most reported food protein amyloid fibrils. Overall, this study demonstrates the upcycling of krill waste protein into amyloid materials with significant material properties, contributing to the resource-efficient and sustainable utilization of marine protein resources.