Published in Applied Research
The zipper structure of the amyloid fibril formed by the yeast protein
Amyloid fibrils - highly organised structures formed when proteins or parts of proteins fold in a certain conformation – have potential as a new ingredient in food, perhaps as a structural component of gels or foams. In living systems, however, formation and accumulation of amyloid aggregates is associated with a range of adverse health effects, from cataracts to Alzheimer’s disease. Research published in Food Chemistry by Lassé et al. in New Zealand examines the properties of amyloid fibrils derived from common food proteins – whey, kidney bean, soy bean and egg white (albumin).
Simulated in vivo digestive conditions, with the relevant enzymes, were used to test proteolysis of fibrils, whilst an in vitro assay determined toxicity at the cellular level. It was found that all of the fibrils tested were resistant to some degree of proteolysis (a factor perhaps related to morphology), meaning that they could persist in whole or in part in the gastrointestinal tract – the researchers point to other studies using disease-related amyloid fibrils fed to mice, demonstrating deposition in the gut and other organ systems. However, when immortalised cell lines were exposed to the food protein fibrils, no adverse effects were recorded, leading to the conclusion that such fibrils are not directly toxic to human cells.
These observations form an important early step in characterising the interactions of artificially created amyloid fibrils with the human body: in order for a substance to be used in food, it must first and foremost be proved safe with regard to consumers’ health. Further in vivo studies may only serve to strengthen the case for amyloid fibrils being a useful component of the toolbox for novel food innovation, rather than simply a cause of degenerative disease.
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