title: Evaluation of protease resistance and toxicity of amyloid-like food fibrils from whey, soy, kidney bean, and egg white.
abstract: The structural properties of amyloid fibrils combined with their highly functional surface chemistry make them an attractive new food ingredient, for example as highly effective gelling agents. However, the toxic role of amyloid fibrils in disease may cause some concern about their food safety because it has not been established unequivocally if consumption of food fibrils poses a health risk to consumers. Here we present a study of amyloid-like fibrils from whey, kidney bean, soy bean, and egg white to partially address this concern. Fibrils showed varied resistance to proteolytic digestion in vitro by either Proteinase K, pepsin or pancreatin. The toxicity of mature fibrils was measured in vitro and compared to native protein, early-stage-fibrillar protein, and sonicated fibrils in two immortalised human cancer cell lines, Caco-2 and Hec-1a. There was no reduction in the viability of either Caco-2 or Hec-1a cells after treatment with a fibril concentration of up to 0.25 mg/mL.
authors: Riddet Institute, Massey University, Palmerston North, New Zealand; Biomolecular Interaction Centre, University of Canterbury, Christchurch, New Zealand; School of Biological Sciences, University of Canterbury, Christchurch, New Zealand. Electronic address: moritz.lasse@canterbury.ac.nz.
authors: Moritz
authors: M
authors: Lassé
authors: Riddet Institute, Massey University, Palmerston North, New Zealand; Food Nutrition & Health Team, Food & Bio-based Products Group, AgResearch Grasslands, Palmerston North, New Zealand.
authors: Dulantha
authors: D
authors: Ulluwishewa
authors: Biomolecular Interaction Centre, University of Canterbury, Christchurch, New Zealand; School of Biological Sciences, University of Canterbury, Christchurch, New Zealand.
authors: Jackie
authors: J
authors: Healy
authors: Protein Science & Engineering Team, Callaghan Innovation, Christchurch and Lower Hutt, New Zealand.
authors: Dion
authors: D
authors: Thompson
authors: Biomolecular Interaction Centre, University of Canterbury, Christchurch, New Zealand; Protein Science & Engineering Team, Callaghan Innovation, Christchurch and Lower Hutt, New Zealand.
authors: Antonia
authors: A
authors: Miller
authors: Riddet Institute, Massey University, Palmerston North, New Zealand; Food Nutrition & Health Team, Food & Bio-based Products Group, AgResearch Grasslands, Palmerston North, New Zealand.
authors: Nicole
authors: N
authors: Roy
authors: Department of Obstetrics and Gynaecology, University of Otago, Christchurch, New Zealand.
authors: Kenny
authors: K
authors: Chitcholtan
authors: Riddet Institute, Massey University, Palmerston North, New Zealand; Biomolecular Interaction Centre, University of Canterbury, Christchurch, New Zealand; Protein Science & Engineering Team, Callaghan Innovation, Christchurch and Lower Hutt, New Zealand; School of Biological Sciences and School of Chemical Sciences, University of Auckland, Auckland, New Zealand.
authors: Juliet A
authors: JA
authors: Gerrard
mesh_terms: D000682:Amyloid / Q000032:analysis / Q000378:metabolism / Q000633:toxicity*; D018938:Caco-2 Cells; D002461:Cell Line, Transformed; D004529:Egg White / Q000737:chemistry*; D004847:Epithelial Cells; D006801:Humans; D010447:Peptide Hydrolases / Q000378:metabolism*; D027805:Phaseolus / Q000737:chemistry*; D059748:Proteolysis; D012639:Seeds / Q000737:chemistry; D013025:Glycine max / Q000737:chemistry*; D000067796:Whey / Q000737:chemistry*
chemical_list: D000682:Amyloid; D010447:Peptide Hydrolases
keywords: Aggregate; Amyloid; Caco-2; Cytotoxicity; Digestibility; Hec-1a; Protein