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Chemical Characterization of a Collagen-Derived Protein Hydrolysate and Biostimulant Activity Assessment of Its Peptidic Components

[Image: see text] Protein hydrolysates (PHs) are plant biostimulants consisting of oligopeptides and free amino acids exploited in agriculture to increase crop productivity. This work aimed to fractionate a commercial collagen-derived protein hydrolysate (CDPH) according to the molecular mass of the...

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Autores principales: Ambrosini, Stefano, Prinsi, Bhakti, Zamboni, Anita, Espen, Luca, Zanzoni, Serena, Santi, Chiara, Varanini, Zeno, Pandolfini, Tiziana
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2022
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9479078/
https://www.ncbi.nlm.nih.gov/pubmed/36039940
http://dx.doi.org/10.1021/acs.jafc.2c04379
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author Ambrosini, Stefano
Prinsi, Bhakti
Zamboni, Anita
Espen, Luca
Zanzoni, Serena
Santi, Chiara
Varanini, Zeno
Pandolfini, Tiziana
author_facet Ambrosini, Stefano
Prinsi, Bhakti
Zamboni, Anita
Espen, Luca
Zanzoni, Serena
Santi, Chiara
Varanini, Zeno
Pandolfini, Tiziana
author_sort Ambrosini, Stefano
collection PubMed
description [Image: see text] Protein hydrolysates (PHs) are plant biostimulants consisting of oligopeptides and free amino acids exploited in agriculture to increase crop productivity. This work aimed to fractionate a commercial collagen-derived protein hydrolysate (CDPH) according to the molecular mass of the peptides and evaluate the bioactivity of different components. First, the CDPH was dialyzed and/or filtrated and analyzed on maize, showing that smaller compounds were particularly active in stimulating lateral root growth. The CDPH was then fractionated through fast protein liquid chromatography and tested on in vitro grown tomatoes proving that all the fractions were bioactive. Furthermore, these fractions were characterized by liquid chromatography–electrospray ionization–tandem mass spectrometry revealing a consensus sequence shared among the identified peptides. Based on this sequence, a synthetic peptide was produced. We assessed its structural similarity with the CDPH, the collagen, and polyproline type II helix by comparing the respective circular dichroism spectra and for the first time, we proved that a signature peptide was as bioactive as the whole CDPH.
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spelling pubmed-94790782022-09-17 Chemical Characterization of a Collagen-Derived Protein Hydrolysate and Biostimulant Activity Assessment of Its Peptidic Components Ambrosini, Stefano Prinsi, Bhakti Zamboni, Anita Espen, Luca Zanzoni, Serena Santi, Chiara Varanini, Zeno Pandolfini, Tiziana J Agric Food Chem [Image: see text] Protein hydrolysates (PHs) are plant biostimulants consisting of oligopeptides and free amino acids exploited in agriculture to increase crop productivity. This work aimed to fractionate a commercial collagen-derived protein hydrolysate (CDPH) according to the molecular mass of the peptides and evaluate the bioactivity of different components. First, the CDPH was dialyzed and/or filtrated and analyzed on maize, showing that smaller compounds were particularly active in stimulating lateral root growth. The CDPH was then fractionated through fast protein liquid chromatography and tested on in vitro grown tomatoes proving that all the fractions were bioactive. Furthermore, these fractions were characterized by liquid chromatography–electrospray ionization–tandem mass spectrometry revealing a consensus sequence shared among the identified peptides. Based on this sequence, a synthetic peptide was produced. We assessed its structural similarity with the CDPH, the collagen, and polyproline type II helix by comparing the respective circular dichroism spectra and for the first time, we proved that a signature peptide was as bioactive as the whole CDPH. American Chemical Society 2022-08-30 2022-09-14 /pmc/articles/PMC9479078/ /pubmed/36039940 http://dx.doi.org/10.1021/acs.jafc.2c04379 Text en © 2022 The Authors. Published by American Chemical Society https://creativecommons.org/licenses/by/4.0/Permits the broadest form of re-use including for commercial purposes, provided that author attribution and integrity are maintained (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Ambrosini, Stefano
Prinsi, Bhakti
Zamboni, Anita
Espen, Luca
Zanzoni, Serena
Santi, Chiara
Varanini, Zeno
Pandolfini, Tiziana
Chemical Characterization of a Collagen-Derived Protein Hydrolysate and Biostimulant Activity Assessment of Its Peptidic Components
title Chemical Characterization of a Collagen-Derived Protein Hydrolysate and Biostimulant Activity Assessment of Its Peptidic Components
title_full Chemical Characterization of a Collagen-Derived Protein Hydrolysate and Biostimulant Activity Assessment of Its Peptidic Components
title_fullStr Chemical Characterization of a Collagen-Derived Protein Hydrolysate and Biostimulant Activity Assessment of Its Peptidic Components
title_full_unstemmed Chemical Characterization of a Collagen-Derived Protein Hydrolysate and Biostimulant Activity Assessment of Its Peptidic Components
title_short Chemical Characterization of a Collagen-Derived Protein Hydrolysate and Biostimulant Activity Assessment of Its Peptidic Components
title_sort chemical characterization of a collagen-derived protein hydrolysate and biostimulant activity assessment of its peptidic components
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9479078/
https://www.ncbi.nlm.nih.gov/pubmed/36039940
http://dx.doi.org/10.1021/acs.jafc.2c04379
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