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

Lassé, Moritz; Ulluwishewa, Dulantha; Healy, Jackie P.; Thompson, Dion; Miller, Antonia Grace; Roy, Nicole C.; Chitcholtan, Kenny; Gerrard, Juliet A.

doi:10.1016/j.foodchem.2015.07.044

Cited by 85 publications

(56 citation statements)

References 39 publications

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“…Most of the proteolytic studies in the literature have been based on the protease resistance of fibrils in the context of amyloidosis [7,35,51,52,53,54]. Recent reports on food fibrils as a potential ingredient in food formulations have shown some extent of resistance of fibrils in whey protein, soy protein, kidney bean isolates, and egg whites, towards proteases such as pepsin, pancreatin, and Proteinase K [55]. Furthermore, comparative studies on crystallin, insulin, and whey protein amyloid fibrils have demonstrated a higher but varying protease resistance of amyloid fibrils towards trypsin, pepsin, and Proteinase K [23].…”

Section: Discussionmentioning

confidence: 99%

Amyloid Fibrils from Hemoglobin

et al. 2017

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Amyloid fibrils are a class of insoluble protein nanofibers that are formed via the self-assembly of a wide range of peptides and proteins. They are increasingly exploited for a broad range of applications in bionanotechnology, such as biosensing and drug delivery, as nanowires, hydrogels, and thin films. Amyloid fibrils have been prepared from many proteins, but there has been no definitive characterization of amyloid fibrils from hemoglobin to date. Here, nanofiber formation was carried out under denaturing conditions using solutions of apo-hemoglobin extracted from bovine waste blood. A characteristic amyloid fibril morphology was confirmed by transmission electron microscopy (TEM) and atomic force microscopy (AFM), with mean fibril dimensions of approximately 5 nm diameter and up to several microns in length. The thioflavin T assay confirmed the presence of β-sheet structures in apo-hemoglobin fibrils, and X-ray fiber diffraction showed the characteristic amyloid cross-β quaternary structure. Apo-hemoglobin nanofibers demonstrated high stability over a range of temperatures (−20 to 80 °C) and pHs (2–10), and were stable in the presence of organic solvents and trypsin, confirming their potential as nanomaterials with versatile applications. This study conclusively demonstrates the formation of amyloid fibrils from hemoglobin for the first time, and also introduces a cost-effective method for amyloid fibril manufacture using meat industry by-products.

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Section: Discussionmentioning

confidence: 99%

Amyloid Fibrils from Hemoglobin

et al. 2017

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“…The effect of pepsin varies with the substrate. AFs produced from whey, kidney bean, soy bean, and egg ovalbumin are partially degraded by pepsin at pH 1.6 with fibrils from whey protein being more resistant to hydrolysis than those from the other tested proteins (Lassé et al., ). In a similar experiment, Bateman, Ye, and Singh () showed that long straight fibrils produced from β‐lactoglobulin are swiftly degraded by pepsin at pH 1.2.…”

Section: Food Protein Amyloids Potentially Have Negative Health Impacmentioning

confidence: 91%

“…Lassé et al. () showed that the viability of enterocyte‐like Caco‐2 cells is only minimally modified by mature fibrils, pre‐fibrillar aggregates, and sonicated fibrils derived from whey, soy, kidney bean, or egg white proteins. Prior to adding amyloid‐like structures in food systems or stimulating their formation it is advisable to verify whether it is safe to apply such structures in products for human consumption.…”

Section: Food Protein Amyloids Potentially Have Negative Health Impacmentioning

confidence: 99%

“…Pancreatin and proteinase K degrade whey, kidney bean, soy bean, and ovalbumin AFs at pH 7.5 to an extent which depends on hydrolysis time, enzyme, and substrate (Lassé et al., ). The native fibrils showed no toxicity towards cell lines including intestinal Caco‐2 and endometrial Hec‐1a cells, except for kidney bean fibrils, which caused a slight decrease (5% TO 10%) in viability of Hec‐1a‐epithelial cells.…”

Section: Food Protein Amyloids Potentially Have Negative Health Impacmentioning

confidence: 99%

“…Intact and digested native fibrils increased the metabolic activity as tested with the WST‐1 reagent with about 20%. It is not clear whether this was due to increased cell proliferation or increased cellular stress, although the authors (Lassé et al., ) suggested that the cells may have been able to use these substrates as an energy source.…”

Section: Food Protein Amyloids Potentially Have Negative Health Impacmentioning

confidence: 99%

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Rational Design of Amyloid‐Like Fibrillary Structures for Tailoring Food Protein Techno‐Functionality and Their Potential Health Implications

Jansens

Rombouts

Grootaert

et al. 2018

Comp Rev Food Sci Food Safe

108

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To control and enhance protein functionality is a major challenge for food scientists. In this context, research on food protein fibril formation, especially amyloid fibril formation, holds much promise. We here first provide a concise overview of conditions, which affect amyloid formation in food proteins. Particular attention is directed towards amyloid core regions because these sequences promote ordered aggregation. Better understanding of this process will be key to tailor the fibril formation process. Especially seeding, that is, adding preformed protein fibrils to protein solutions to accelerate fibril formation holds promise to tailor aggregation and fibril techno‐functionality. Some studies have already indicated that food protein fibrillation indeed improves their techno‐functionality. However, much more research is necessary to establish whether protein fibrils are useful in complex food systems and whether and to what extent they resist food processing unit operations. In this review the effect of amyloid formation on gelation, interfacial properties, foaming, and emulsification is discussed. Despite their prevalent role as functional structures, amyloids also receive a lot of attention due to their association with protein deposition diseases, prompting us to thoroughly investigate the potential health impact of amyloid‐like aggregates in food. A literature review on the effect of the different stages of the human digestive process on amyloid toxicity leads us to conclude that food‐derived amyloid fibrils (even those with potential pathogenic properties) very likely have minimal impact on human health. Nevertheless, prior to wide‐spread application of the technology, it is highly advisable to further verify the lack of toxicity of food‐derived amyloid fibrils.

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