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Valorization of Apple Peels through the Study of the Effects on the Amyloid Aggregation Process of κ-Casein
Waste valorization represents one of the main social challenges when promoting a circular economy and environmental sustainability. Here, we evaluated the effect of the polyphenols extracted from apple peels, normally disposed of as waste, on the amyloid aggregation process of κ-casein from bovine m...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8073991/ https://www.ncbi.nlm.nih.gov/pubmed/33921801 http://dx.doi.org/10.3390/molecules26082371 |
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author | Guarrasi, Valeria Rappa, Giacoma Cinzia Costa, Maria Assunta Librizzi, Fabio Raimondo, Marco Di Stefano, Vita Germanà, Maria Antonietta Vilasi, Silvia |
author_facet | Guarrasi, Valeria Rappa, Giacoma Cinzia Costa, Maria Assunta Librizzi, Fabio Raimondo, Marco Di Stefano, Vita Germanà, Maria Antonietta Vilasi, Silvia |
author_sort | Guarrasi, Valeria |
collection | PubMed |
description | Waste valorization represents one of the main social challenges when promoting a circular economy and environmental sustainability. Here, we evaluated the effect of the polyphenols extracted from apple peels, normally disposed of as waste, on the amyloid aggregation process of κ-casein from bovine milk, a well-used amyloidogenic model system. The effect of the apple peel extract on protein aggregation was examined using a thioflavin T fluorescence assay, Congo red binding assay, circular dichroism, light scattering, and atomic force microscopy. We found that the phenolic extract from the peel of apples of the cultivar “Fuji”, cultivated in Sicily (Caltavuturo, Italy), inhibited κ-casein fibril formation in a dose-dependent way. In particular, we found that the extract significantly reduced the protein aggregation rate and inhibited the secondary structure reorganization that accompanies κ-casein amyloid formation. Protein-aggregated species resulting from the incubation of κ-casein in the presence of polyphenols under amyloid aggregation conditions were reduced in number and different in morphology. |
format | Online Article Text |
id | pubmed-8073991 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-80739912021-04-27 Valorization of Apple Peels through the Study of the Effects on the Amyloid Aggregation Process of κ-Casein Guarrasi, Valeria Rappa, Giacoma Cinzia Costa, Maria Assunta Librizzi, Fabio Raimondo, Marco Di Stefano, Vita Germanà, Maria Antonietta Vilasi, Silvia Molecules Article Waste valorization represents one of the main social challenges when promoting a circular economy and environmental sustainability. Here, we evaluated the effect of the polyphenols extracted from apple peels, normally disposed of as waste, on the amyloid aggregation process of κ-casein from bovine milk, a well-used amyloidogenic model system. The effect of the apple peel extract on protein aggregation was examined using a thioflavin T fluorescence assay, Congo red binding assay, circular dichroism, light scattering, and atomic force microscopy. We found that the phenolic extract from the peel of apples of the cultivar “Fuji”, cultivated in Sicily (Caltavuturo, Italy), inhibited κ-casein fibril formation in a dose-dependent way. In particular, we found that the extract significantly reduced the protein aggregation rate and inhibited the secondary structure reorganization that accompanies κ-casein amyloid formation. Protein-aggregated species resulting from the incubation of κ-casein in the presence of polyphenols under amyloid aggregation conditions were reduced in number and different in morphology. MDPI 2021-04-19 /pmc/articles/PMC8073991/ /pubmed/33921801 http://dx.doi.org/10.3390/molecules26082371 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Guarrasi, Valeria Rappa, Giacoma Cinzia Costa, Maria Assunta Librizzi, Fabio Raimondo, Marco Di Stefano, Vita Germanà, Maria Antonietta Vilasi, Silvia Valorization of Apple Peels through the Study of the Effects on the Amyloid Aggregation Process of κ-Casein |
title | Valorization of Apple Peels through the Study of the Effects on the Amyloid Aggregation Process of κ-Casein |
title_full | Valorization of Apple Peels through the Study of the Effects on the Amyloid Aggregation Process of κ-Casein |
title_fullStr | Valorization of Apple Peels through the Study of the Effects on the Amyloid Aggregation Process of κ-Casein |
title_full_unstemmed | Valorization of Apple Peels through the Study of the Effects on the Amyloid Aggregation Process of κ-Casein |
title_short | Valorization of Apple Peels through the Study of the Effects on the Amyloid Aggregation Process of κ-Casein |
title_sort | valorization of apple peels through the study of the effects on the amyloid aggregation process of κ-casein |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8073991/ https://www.ncbi.nlm.nih.gov/pubmed/33921801 http://dx.doi.org/10.3390/molecules26082371 |
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