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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...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2022
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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. |
format | Online Article Text |
id | pubmed-9479078 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | American Chemical Society |
record_format | MEDLINE/PubMed |
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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