Porcine placenta hydrolysate as an alternate functional food ingredient: In vitro antioxidant and antibacterial assessments.

The production of bioactive peptides from animal-based raw materials highly depends on enzymatic hydrolysis. Porcine placenta is an underutilized biomass in Thailand's pig farms, yet it is still a source of proteins and beneficial compounds. Porcine placenta could be used as a protein substrate...

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Autores principales: Phanthipha Laosam, Worawan Panpipat, Gorawit Yusakul, Ling-Zhi Cheong, Manat Chaijan
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Publicado: Public Library of Science (PLoS) 2021
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spelling oai:doaj.org-article:6748d3743aca44b08d36e1062eee6a452021-12-02T20:16:35ZPorcine placenta hydrolysate as an alternate functional food ingredient: In vitro antioxidant and antibacterial assessments.1932-620310.1371/journal.pone.0258445https://doaj.org/article/6748d3743aca44b08d36e1062eee6a452021-01-01T00:00:00Zhttps://doi.org/10.1371/journal.pone.0258445https://doaj.org/toc/1932-6203The production of bioactive peptides from animal-based raw materials highly depends on enzymatic hydrolysis. Porcine placenta is an underutilized biomass in Thailand's pig farms, yet it is still a source of proteins and beneficial compounds. Porcine placenta could be used as a protein substrate for the production of enzymatic hydrolysate, which could be employed as a functional food ingredient in the future. The goal of this study was to enzymatically produce porcine placenta hydrolysates (PPH) using three commercial enzymes (Alcalase, Flavouzyme, and papain) and evaluate their in vitro antioxidant and antibacterial activity. The degree of hydrolysis (DH) increased as the enzyme load and hydrolysis time increased, but the DH was governed by the enzyme class. The maximum DH was found after using 10% enzyme for 20 min of hydrolysis (36.60%, 31.40%, and 29.81% for Alcalase, Flavouzyme, and papain). Depending on the enzyme type and DH, peptides of various sizes (0.40-323.56 kDa) were detected in all PPH. PPH created with Alcalase had an excellent reducing capacity and metal chelating ability (p < 0.05), whereas PPH made with Flavourzyme and Papain had higher DPPH• and ABTS•+ inhibitory activities (p < 0.05). Papain-derived PPH also had a strong antibacterial effect against Staphylococcus aureus and Escherichia coli, with clear zone values of 17.20 mm and 14.00 mm, respectively (p < 0.05). When PPH was transported via a gastrointestinal tract model system, its antioxidative characteristics were altered. PPH's properties and bioactivities were thus influenced by the enzyme type, enzyme concentration, and hydrolysis time used. Therefore, PPH produced from porcine placenta can be categorized as an antioxidant and antibacterial alternative.Phanthipha LaosamWorawan PanpipatGorawit YusakulLing-Zhi CheongManat ChaijanPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 16, Iss 10, p e0258445 (2021)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Phanthipha Laosam
Worawan Panpipat
Gorawit Yusakul
Ling-Zhi Cheong
Manat Chaijan
Porcine placenta hydrolysate as an alternate functional food ingredient: In vitro antioxidant and antibacterial assessments.
description The production of bioactive peptides from animal-based raw materials highly depends on enzymatic hydrolysis. Porcine placenta is an underutilized biomass in Thailand's pig farms, yet it is still a source of proteins and beneficial compounds. Porcine placenta could be used as a protein substrate for the production of enzymatic hydrolysate, which could be employed as a functional food ingredient in the future. The goal of this study was to enzymatically produce porcine placenta hydrolysates (PPH) using three commercial enzymes (Alcalase, Flavouzyme, and papain) and evaluate their in vitro antioxidant and antibacterial activity. The degree of hydrolysis (DH) increased as the enzyme load and hydrolysis time increased, but the DH was governed by the enzyme class. The maximum DH was found after using 10% enzyme for 20 min of hydrolysis (36.60%, 31.40%, and 29.81% for Alcalase, Flavouzyme, and papain). Depending on the enzyme type and DH, peptides of various sizes (0.40-323.56 kDa) were detected in all PPH. PPH created with Alcalase had an excellent reducing capacity and metal chelating ability (p < 0.05), whereas PPH made with Flavourzyme and Papain had higher DPPH• and ABTS•+ inhibitory activities (p < 0.05). Papain-derived PPH also had a strong antibacterial effect against Staphylococcus aureus and Escherichia coli, with clear zone values of 17.20 mm and 14.00 mm, respectively (p < 0.05). When PPH was transported via a gastrointestinal tract model system, its antioxidative characteristics were altered. PPH's properties and bioactivities were thus influenced by the enzyme type, enzyme concentration, and hydrolysis time used. Therefore, PPH produced from porcine placenta can be categorized as an antioxidant and antibacterial alternative.
format article
author Phanthipha Laosam
Worawan Panpipat
Gorawit Yusakul
Ling-Zhi Cheong
Manat Chaijan
author_facet Phanthipha Laosam
Worawan Panpipat
Gorawit Yusakul
Ling-Zhi Cheong
Manat Chaijan
author_sort Phanthipha Laosam
title Porcine placenta hydrolysate as an alternate functional food ingredient: In vitro antioxidant and antibacterial assessments.
title_short Porcine placenta hydrolysate as an alternate functional food ingredient: In vitro antioxidant and antibacterial assessments.
title_full Porcine placenta hydrolysate as an alternate functional food ingredient: In vitro antioxidant and antibacterial assessments.
title_fullStr Porcine placenta hydrolysate as an alternate functional food ingredient: In vitro antioxidant and antibacterial assessments.
title_full_unstemmed Porcine placenta hydrolysate as an alternate functional food ingredient: In vitro antioxidant and antibacterial assessments.
title_sort porcine placenta hydrolysate as an alternate functional food ingredient: in vitro antioxidant and antibacterial assessments.
publisher Public Library of Science (PLoS)
publishDate 2021
url https://doaj.org/article/6748d3743aca44b08d36e1062eee6a45
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AT gorawityusakul porcineplacentahydrolysateasanalternatefunctionalfoodingredientinvitroantioxidantandantibacterialassessments
AT lingzhicheong porcineplacentahydrolysateasanalternatefunctionalfoodingredientinvitroantioxidantandantibacterialassessments
AT manatchaijan porcineplacentahydrolysateasanalternatefunctionalfoodingredientinvitroantioxidantandantibacterialassessments
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