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Antiproliferative Rapeseed Defatted Meal Protein and Their Hydrolysates on MCF-7 Breast Cancer Cells and Human Fibroblasts
Defatted rapeseed meal (DRM) is a sub-valorized agro-industrial by-product, with a high protein content whose peptides could have potential anticancer activity against cancer cell lines. The objective of the present study is to obtain an enzymatic hydrolysate of rapeseed protein that inhibits prolif...
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/PMC7913290/ https://www.ncbi.nlm.nih.gov/pubmed/33546198 http://dx.doi.org/10.3390/foods10020309 |
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author | Ferrero, Romina L. Soto-Maldonado, Carmen Weinstein-Oppenheimer, Caroline Cabrera-Muñoz, Zaida Zúñiga-Hansen, María Elvira |
author_facet | Ferrero, Romina L. Soto-Maldonado, Carmen Weinstein-Oppenheimer, Caroline Cabrera-Muñoz, Zaida Zúñiga-Hansen, María Elvira |
author_sort | Ferrero, Romina L. |
collection | PubMed |
description | Defatted rapeseed meal (DRM) is a sub-valorized agro-industrial by-product, with a high protein content whose peptides could have potential anticancer activity against cancer cell lines. The objective of the present study is to obtain an enzymatic hydrolysate of rapeseed protein that inhibits proliferation on a breast cancer cell line (MCF-7), but not healthy human fibroblast cells. The DRM was solubilized in an alkaline medium to obtain an alkaline rapeseed extract (RAE). Acid precipitation of the proteins contained in RAE recovered a rapeseed protein isolate (RPI). To produce protein hydrolysates, two alkaline protease and different enzyme/substrate ratios were used. All the protein hydrolysates showed antiproliferative activity on MCF-7 cells. However, only the hydrolysate recovered from the enzymatic hydrolysis of RPI (Degree of hydrolysis (DH ) between 8.5 and 9% (DH1)) did not affect human fibroblast cells, inhibiting 83.9% of MCF-7 cells’ proliferation and showing a mass yield of 22.9% (based on the initial DRM). The SDS-PAGE gel revealed that DH1 was composed mainly of 10 kDa peptides and, to a lesser extent, 5 and 2 kDa. It is concluded that DH1 is a promising peptide extract for future research as a putative anti-breast cancer agent. |
format | Online Article Text |
id | pubmed-7913290 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-79132902021-02-28 Antiproliferative Rapeseed Defatted Meal Protein and Their Hydrolysates on MCF-7 Breast Cancer Cells and Human Fibroblasts Ferrero, Romina L. Soto-Maldonado, Carmen Weinstein-Oppenheimer, Caroline Cabrera-Muñoz, Zaida Zúñiga-Hansen, María Elvira Foods Article Defatted rapeseed meal (DRM) is a sub-valorized agro-industrial by-product, with a high protein content whose peptides could have potential anticancer activity against cancer cell lines. The objective of the present study is to obtain an enzymatic hydrolysate of rapeseed protein that inhibits proliferation on a breast cancer cell line (MCF-7), but not healthy human fibroblast cells. The DRM was solubilized in an alkaline medium to obtain an alkaline rapeseed extract (RAE). Acid precipitation of the proteins contained in RAE recovered a rapeseed protein isolate (RPI). To produce protein hydrolysates, two alkaline protease and different enzyme/substrate ratios were used. All the protein hydrolysates showed antiproliferative activity on MCF-7 cells. However, only the hydrolysate recovered from the enzymatic hydrolysis of RPI (Degree of hydrolysis (DH ) between 8.5 and 9% (DH1)) did not affect human fibroblast cells, inhibiting 83.9% of MCF-7 cells’ proliferation and showing a mass yield of 22.9% (based on the initial DRM). The SDS-PAGE gel revealed that DH1 was composed mainly of 10 kDa peptides and, to a lesser extent, 5 and 2 kDa. It is concluded that DH1 is a promising peptide extract for future research as a putative anti-breast cancer agent. MDPI 2021-02-03 /pmc/articles/PMC7913290/ /pubmed/33546198 http://dx.doi.org/10.3390/foods10020309 Text en © 2021 by the authors. 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 (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Ferrero, Romina L. Soto-Maldonado, Carmen Weinstein-Oppenheimer, Caroline Cabrera-Muñoz, Zaida Zúñiga-Hansen, María Elvira Antiproliferative Rapeseed Defatted Meal Protein and Their Hydrolysates on MCF-7 Breast Cancer Cells and Human Fibroblasts |
title | Antiproliferative Rapeseed Defatted Meal Protein and Their Hydrolysates on MCF-7 Breast Cancer Cells and Human Fibroblasts |
title_full | Antiproliferative Rapeseed Defatted Meal Protein and Their Hydrolysates on MCF-7 Breast Cancer Cells and Human Fibroblasts |
title_fullStr | Antiproliferative Rapeseed Defatted Meal Protein and Their Hydrolysates on MCF-7 Breast Cancer Cells and Human Fibroblasts |
title_full_unstemmed | Antiproliferative Rapeseed Defatted Meal Protein and Their Hydrolysates on MCF-7 Breast Cancer Cells and Human Fibroblasts |
title_short | Antiproliferative Rapeseed Defatted Meal Protein and Their Hydrolysates on MCF-7 Breast Cancer Cells and Human Fibroblasts |
title_sort | antiproliferative rapeseed defatted meal protein and their hydrolysates on mcf-7 breast cancer cells and human fibroblasts |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7913290/ https://www.ncbi.nlm.nih.gov/pubmed/33546198 http://dx.doi.org/10.3390/foods10020309 |
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