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Enzymatic production of bioactive peptides from scotta, an exhausted by-product of ricotta cheese processing
The present work reports the enzymatic valorisation of the protein fraction of scotta, a dairy by-product representing the exhausted liquid residue of ricotta production. Scotta was subjected to ultra-filtration with membrane cut-offs from 500 to 4 kDa and the obtained protein-enriched fractions wer...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6936807/ https://www.ncbi.nlm.nih.gov/pubmed/31887121 http://dx.doi.org/10.1371/journal.pone.0226834 |
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author | Monari, Stefania Ferri, Maura Russo, Claudio Prandi, Barbara Tedeschi, Tullia Bellucci, Paolo Zambrini, Angelo Vittorio Donati, Emanuela Tassoni, Annalisa |
author_facet | Monari, Stefania Ferri, Maura Russo, Claudio Prandi, Barbara Tedeschi, Tullia Bellucci, Paolo Zambrini, Angelo Vittorio Donati, Emanuela Tassoni, Annalisa |
author_sort | Monari, Stefania |
collection | PubMed |
description | The present work reports the enzymatic valorisation of the protein fraction of scotta, a dairy by-product representing the exhausted liquid residue of ricotta production. Scotta was subjected to ultra-filtration with membrane cut-offs from 500 to 4 kDa and the obtained protein-enriched fractions were used for the optimization of enzyme-based digestions aimed at producing potentially bioactive peptides. Nine different commercial proteases were tested and the best digestion conditions were selected based on protein yield, fraction bioactivity and foreseen scale up processing costs. Scale up of the 3% Pancreatin or 5% Papain processes was performed up to 2 L (37°C or 60°C respectively, 1 h incubation), and the digestion efficiency increased with the reaction volume as well as antioxidant activity (up to 60 gBSA eq/L and to 1.7 gAA eq/L). Retentate 1 digested fractions also showed, for the first time in dairy-based peptides, anti-tyrosinase activity, up to 0.14 gKA eq/L. Digested proteins were sub-fractionated by means of physical membrane separations and 30–10 kDa fraction from Papain treatment showed the highest antioxidant and anti-tyrosinase activities. The peptide sequence of the most bioactive fractions was achieved. |
format | Online Article Text |
id | pubmed-6936807 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-69368072020-01-07 Enzymatic production of bioactive peptides from scotta, an exhausted by-product of ricotta cheese processing Monari, Stefania Ferri, Maura Russo, Claudio Prandi, Barbara Tedeschi, Tullia Bellucci, Paolo Zambrini, Angelo Vittorio Donati, Emanuela Tassoni, Annalisa PLoS One Research Article The present work reports the enzymatic valorisation of the protein fraction of scotta, a dairy by-product representing the exhausted liquid residue of ricotta production. Scotta was subjected to ultra-filtration with membrane cut-offs from 500 to 4 kDa and the obtained protein-enriched fractions were used for the optimization of enzyme-based digestions aimed at producing potentially bioactive peptides. Nine different commercial proteases were tested and the best digestion conditions were selected based on protein yield, fraction bioactivity and foreseen scale up processing costs. Scale up of the 3% Pancreatin or 5% Papain processes was performed up to 2 L (37°C or 60°C respectively, 1 h incubation), and the digestion efficiency increased with the reaction volume as well as antioxidant activity (up to 60 gBSA eq/L and to 1.7 gAA eq/L). Retentate 1 digested fractions also showed, for the first time in dairy-based peptides, anti-tyrosinase activity, up to 0.14 gKA eq/L. Digested proteins were sub-fractionated by means of physical membrane separations and 30–10 kDa fraction from Papain treatment showed the highest antioxidant and anti-tyrosinase activities. The peptide sequence of the most bioactive fractions was achieved. Public Library of Science 2019-12-30 /pmc/articles/PMC6936807/ /pubmed/31887121 http://dx.doi.org/10.1371/journal.pone.0226834 Text en © 2019 Monari et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Research Article Monari, Stefania Ferri, Maura Russo, Claudio Prandi, Barbara Tedeschi, Tullia Bellucci, Paolo Zambrini, Angelo Vittorio Donati, Emanuela Tassoni, Annalisa Enzymatic production of bioactive peptides from scotta, an exhausted by-product of ricotta cheese processing |
title | Enzymatic production of bioactive peptides from scotta, an exhausted by-product of ricotta cheese processing |
title_full | Enzymatic production of bioactive peptides from scotta, an exhausted by-product of ricotta cheese processing |
title_fullStr | Enzymatic production of bioactive peptides from scotta, an exhausted by-product of ricotta cheese processing |
title_full_unstemmed | Enzymatic production of bioactive peptides from scotta, an exhausted by-product of ricotta cheese processing |
title_short | Enzymatic production of bioactive peptides from scotta, an exhausted by-product of ricotta cheese processing |
title_sort | enzymatic production of bioactive peptides from scotta, an exhausted by-product of ricotta cheese processing |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6936807/ https://www.ncbi.nlm.nih.gov/pubmed/31887121 http://dx.doi.org/10.1371/journal.pone.0226834 |
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