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Evaluation of protease resistance and toxicity of amyloid-like food fibrils from whey, soy, kidney bean, and egg white

journal contribution
posted on 2023-05-03, 18:31 authored by Moritiz Lassé, Dulantha UlluwishewaDulantha Ulluwishewa, Jackie Healy, Dion Thompson, Antonia Miller, Nicole Roy, Kenny Chitcholtan, Juliet Gerrard
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.

History

Rights statement

© 2015 Elsevier Ltd. All rights reserved.

Language

  • English

Does this contain Māori information or data?

  • No

Publisher

Elsevier

Journal title

Food Chemistry

ISSN

0308-8146

Citation

Lassé, M., Ulluwishewa, D., Healy, J., Thompson, D., Miller, A., Roy, N., Chitcholtan, K., & Gerrard, J. A. (2016). Evaluation of protease resistance and toxicity of amyloid-like food fibrils from whey, soy, kidney bean, and egg white. Food Chemistry, 192, 491-498.

Contract number

A21483

Job code

11352

Report number

FBP 56108||FBP 45153

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