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TitleEvaluation of protease resistance and toxicity of amyloid-like food fibrils from whey, soy, kidney bean, and egg white
Publication TypeJournal Article
Year of Publication2015
AuthorsLassé, M., Ulluwishewa D., Healy J., Thompson D., Miller A., Roy N., Chitcholtan K., and Gerrard J.A.
JournalFood Chemistry
Pagination491 - 498
Date Published2015
ISSN03088146 (ISSN)
KeywordsAggregates, amyloid, Amyloid-like fibril, Caco-2, cancer cell line, cell culture, cell viability, controlled study, cytotoxicity, Digestibility, egg white, Functional surfaces, Glycoproteins, Health risks, Hec-1a, human, Human cancer cells, human cell, immortalized cell line, in vitro study, pancreatin, pepsin A, Phaseolus vulgaris, protein degradation, proteinase, proteinase K, Proteins, Proteolytic digestion, soybean, Surface chemistry, Toxicity, ultrasound, whey
AbstractAbstract 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. © 2015 Elsevier Ltd.

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