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Assessment of Food By-Products’ Potential for Simultaneous Binding of Aflatoxin B1 and Zearalenone
In this study, eight food by-products were investigated as biosorbent approaches in removing mycotoxin load towards potential dietary inclusion in animal feed. Among these food-derived by-products, grape seed (GSM) and seabuckthorn (SBM) meals showed the most promising binding capacity for Aflatoxin...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7822050/ https://www.ncbi.nlm.nih.gov/pubmed/33374968 http://dx.doi.org/10.3390/toxins13010002 |
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author | Palade, Laurentiu Mihai Dore, Madalina Ioana Marin, Daniela Eliza Rotar, Mircea Catalin Taranu, Ionelia |
author_facet | Palade, Laurentiu Mihai Dore, Madalina Ioana Marin, Daniela Eliza Rotar, Mircea Catalin Taranu, Ionelia |
author_sort | Palade, Laurentiu Mihai |
collection | PubMed |
description | In this study, eight food by-products were investigated as biosorbent approaches in removing mycotoxin load towards potential dietary inclusion in animal feed. Among these food-derived by-products, grape seed (GSM) and seabuckthorn (SBM) meals showed the most promising binding capacity for Aflatoxin B1 (AFB1) and Zearalenone (ZEA), measured as percent of adsorbed mycotoxin. Furthermore, we explored the mycotoxin sequestering potential by screening the effect of time, concentration, temperature and pH. Comparative binding efficacy was addressed by carrying out adsorption experiments in vitro. The highest mycotoxin adsorption was attained using 30 mg of by-product for both GSM (85.9% AFB1 and 83.7% ZEA) and SBM (68% AFB1 and 84.5% ZEA). Optimal settings for the experimental factors were predicted employing the response surface design. GSM was estimated to adsorb AFB1 optimally at a concentration of 29 mg/mL, pH 5.95 and 33.6 °C, and ZEA using 28 mg/mL at pH 5.76 and 31.7 °C. Favorable adsorption of AFB1 was estimated at 37.5 mg of SBM (pH 8.1; 35.6 °C), and of ZEA at 30.2 mg of SBM (pH 5.6; 29.3 °C). Overall, GSM revealed a higher binding capacity compared with SBM. In addition, the two by-products showed different specificity for the binary–mycotoxin system, with SBM having higher affinity towards ZEA than AFB1 (K(f) = 0.418 and 1/n = 0.213 vs. K(f) = 0.217 and 1/n = 0.341) and GSM for AFB1 in comparison with ZEA (K(f) = 0.367 and 1/n = 0.248 vs. K(f) = 0.343 and 1/n = 0.264). In conclusion, this study suggests that GSM and SBM represent viable alternatives to commercial biosorbent products. |
format | Online Article Text |
id | pubmed-7822050 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-78220502021-01-23 Assessment of Food By-Products’ Potential for Simultaneous Binding of Aflatoxin B1 and Zearalenone Palade, Laurentiu Mihai Dore, Madalina Ioana Marin, Daniela Eliza Rotar, Mircea Catalin Taranu, Ionelia Toxins (Basel) Article In this study, eight food by-products were investigated as biosorbent approaches in removing mycotoxin load towards potential dietary inclusion in animal feed. Among these food-derived by-products, grape seed (GSM) and seabuckthorn (SBM) meals showed the most promising binding capacity for Aflatoxin B1 (AFB1) and Zearalenone (ZEA), measured as percent of adsorbed mycotoxin. Furthermore, we explored the mycotoxin sequestering potential by screening the effect of time, concentration, temperature and pH. Comparative binding efficacy was addressed by carrying out adsorption experiments in vitro. The highest mycotoxin adsorption was attained using 30 mg of by-product for both GSM (85.9% AFB1 and 83.7% ZEA) and SBM (68% AFB1 and 84.5% ZEA). Optimal settings for the experimental factors were predicted employing the response surface design. GSM was estimated to adsorb AFB1 optimally at a concentration of 29 mg/mL, pH 5.95 and 33.6 °C, and ZEA using 28 mg/mL at pH 5.76 and 31.7 °C. Favorable adsorption of AFB1 was estimated at 37.5 mg of SBM (pH 8.1; 35.6 °C), and of ZEA at 30.2 mg of SBM (pH 5.6; 29.3 °C). Overall, GSM revealed a higher binding capacity compared with SBM. In addition, the two by-products showed different specificity for the binary–mycotoxin system, with SBM having higher affinity towards ZEA than AFB1 (K(f) = 0.418 and 1/n = 0.213 vs. K(f) = 0.217 and 1/n = 0.341) and GSM for AFB1 in comparison with ZEA (K(f) = 0.367 and 1/n = 0.248 vs. K(f) = 0.343 and 1/n = 0.264). In conclusion, this study suggests that GSM and SBM represent viable alternatives to commercial biosorbent products. MDPI 2020-12-22 /pmc/articles/PMC7822050/ /pubmed/33374968 http://dx.doi.org/10.3390/toxins13010002 Text en © 2020 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 Palade, Laurentiu Mihai Dore, Madalina Ioana Marin, Daniela Eliza Rotar, Mircea Catalin Taranu, Ionelia Assessment of Food By-Products’ Potential for Simultaneous Binding of Aflatoxin B1 and Zearalenone |
title | Assessment of Food By-Products’ Potential for Simultaneous Binding of Aflatoxin B1 and Zearalenone |
title_full | Assessment of Food By-Products’ Potential for Simultaneous Binding of Aflatoxin B1 and Zearalenone |
title_fullStr | Assessment of Food By-Products’ Potential for Simultaneous Binding of Aflatoxin B1 and Zearalenone |
title_full_unstemmed | Assessment of Food By-Products’ Potential for Simultaneous Binding of Aflatoxin B1 and Zearalenone |
title_short | Assessment of Food By-Products’ Potential for Simultaneous Binding of Aflatoxin B1 and Zearalenone |
title_sort | assessment of food by-products’ potential for simultaneous binding of aflatoxin b1 and zearalenone |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7822050/ https://www.ncbi.nlm.nih.gov/pubmed/33374968 http://dx.doi.org/10.3390/toxins13010002 |
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