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Enzymatic production of bioactive peptides from scotta, an exhausted by-product of ricotta cheese processing

TitoloEnzymatic production of bioactive peptides from scotta, an exhausted by-product of ricotta cheese processing
Tipo di pubblicazioneArticolo su Rivista peer-reviewed
Anno di Pubblicazione2019
AutoriMonari, S., Ferri M., Russo C., Prandi B., Tedeschi T., Bellucci P., Zambrini A.V., Donati E., and Tassoni A.
RivistaPLoS ONE
Volume14
ISSN19326203
Abstract

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 proteinenriched 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. © 2019 Monari et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

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URLhttps://www.scopus.com/inward/record.uri?eid=2-s2.0-85077319468&doi=10.1371%2fjournal.pone.0226834&partnerID=40&md5=8ce51eafb2b9fe9b2a9f2d81c6a253c2
DOI10.1371/journal.pone.0226834
Citation KeyMonari2019