Nuclei-induced formation of amyloid fibrils in whey protein: Effects of enzyme hydrolysis on the ability of nuclei to induce fibril formation

Abstract

Homogeneous and secondary nuclei (HN and SN) are aggregates formed at different stages of whey protein isolate (WPI) self-assembly. More fibrils can form when HN/SN are added as nuclei than when WPI self-assembles. We evaluated the effect of hydrolysis treatment on fibril-induction ability of nuclei derived from WPI, and investigated the relationship between induction ability and nuclear structure. Hydrolyzed SN-induced 9.47% more WPI fibrils than unhydrolyzed SN-induced. Infrared spectroscopy, X-ray diffraction analysis, and atomic force microscopy were used to examine the structural changes in hydrolyzed nuclei and the fibrils induced using these nuclei. We concluded that hydrolysis treatment led to a looser inter-β-sheet packaging in nuclei by increasing the inter-β-sheet distance. The inter-β-sheet distance of cross-β structure was a key determinant of fibril-induction ability of nuclei, which could be enhanced when inter-β-sheet structure was moderately loose. This research may provide a theoretical basis for the mechanism of nuclei-induced WPI fibrillation.