Potential Biological Activities of Peptides Generated during Casein Proteolysis by Curly Kale (<i>Brassica oleracea</i> L. var. <i>sabellica</i> L.) Leaf Extract: An In Silico Preliminary Study

This study is a brief report on the proteolytic activity of curly kale leaf extract against casein. Casein degradation products and an in silico analysis of the biological activity of the peptides obtained was performed. The efficiency of casein hydrolysis by curly kale extract was determined using...

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Autores principales: Magdalena Polak-Berecka, Magdalena Michalak-Tomczyk, Katarzyna Skrzypczak, Katarzyna Michalak, Kamila Rachwał, Adam Waśko
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spelling oai:doaj.org-article:d90175ff77864d5ab3e30ebf458ed0642021-11-25T17:36:51ZPotential Biological Activities of Peptides Generated during Casein Proteolysis by Curly Kale (<i>Brassica oleracea</i> L. var. <i>sabellica</i> L.) Leaf Extract: An In Silico Preliminary Study10.3390/foods101128772304-8158https://doaj.org/article/d90175ff77864d5ab3e30ebf458ed0642021-11-01T00:00:00Zhttps://www.mdpi.com/2304-8158/10/11/2877https://doaj.org/toc/2304-8158This study is a brief report on the proteolytic activity of curly kale leaf extract against casein. Casein degradation products and an in silico analysis of the biological activity of the peptides obtained was performed. The efficiency of casein hydrolysis by curly kale extract was determined using SDS–PAGE and by peptide concentration determination. The pattern of the enzymatic activity was determined by MALDI–TOF MS analysis. The results showed that α- and β-casein were more resistant to curly kale extract hydrolysis, whereas κ-casein was absent in the protein profile after 8 h of proteolysis, and all casein fractions were completely hydrolyzed after 24 h of incubation. Based on sequence analysis, seven peptides were identified, with molecular mass in the range of 1151–3024 Da. All the peptides were products of β-casein hydrolysis. The identified amino acid sequences were analyzed in BIOPEP, MBPDB, and FeptideDB databases in order to detect the potential activities of the peptides. In silico analysis suggests that the β-casein-derived peptides possess sequences of peptides with ACE inhibitory, antioxidant, dipeptidyl peptidase IV inhibitory, antithrombotic, immunomodulatory, and antiamnesic bioactivity. Our study was first to evaluate the possibility of applying curly kale leaf extract to generate biopeptides through β-casein hydrolysis.Magdalena Polak-BereckaMagdalena Michalak-TomczykKatarzyna SkrzypczakKatarzyna MichalakKamila RachwałAdam WaśkoMDPI AGarticlebioactive peptidescaseincurly kaleMALDI–TOFChemical technologyTP1-1185ENFoods, Vol 10, Iss 2877, p 2877 (2021)
institution DOAJ
collection DOAJ
language EN
topic bioactive peptides
casein
curly kale
MALDI–TOF
Chemical technology
TP1-1185
spellingShingle bioactive peptides
casein
curly kale
MALDI–TOF
Chemical technology
TP1-1185
Magdalena Polak-Berecka
Magdalena Michalak-Tomczyk
Katarzyna Skrzypczak
Katarzyna Michalak
Kamila Rachwał
Adam Waśko
Potential Biological Activities of Peptides Generated during Casein Proteolysis by Curly Kale (<i>Brassica oleracea</i> L. var. <i>sabellica</i> L.) Leaf Extract: An In Silico Preliminary Study
description This study is a brief report on the proteolytic activity of curly kale leaf extract against casein. Casein degradation products and an in silico analysis of the biological activity of the peptides obtained was performed. The efficiency of casein hydrolysis by curly kale extract was determined using SDS–PAGE and by peptide concentration determination. The pattern of the enzymatic activity was determined by MALDI–TOF MS analysis. The results showed that α- and β-casein were more resistant to curly kale extract hydrolysis, whereas κ-casein was absent in the protein profile after 8 h of proteolysis, and all casein fractions were completely hydrolyzed after 24 h of incubation. Based on sequence analysis, seven peptides were identified, with molecular mass in the range of 1151–3024 Da. All the peptides were products of β-casein hydrolysis. The identified amino acid sequences were analyzed in BIOPEP, MBPDB, and FeptideDB databases in order to detect the potential activities of the peptides. In silico analysis suggests that the β-casein-derived peptides possess sequences of peptides with ACE inhibitory, antioxidant, dipeptidyl peptidase IV inhibitory, antithrombotic, immunomodulatory, and antiamnesic bioactivity. Our study was first to evaluate the possibility of applying curly kale leaf extract to generate biopeptides through β-casein hydrolysis.
format article
author Magdalena Polak-Berecka
Magdalena Michalak-Tomczyk
Katarzyna Skrzypczak
Katarzyna Michalak
Kamila Rachwał
Adam Waśko
author_facet Magdalena Polak-Berecka
Magdalena Michalak-Tomczyk
Katarzyna Skrzypczak
Katarzyna Michalak
Kamila Rachwał
Adam Waśko
author_sort Magdalena Polak-Berecka
title Potential Biological Activities of Peptides Generated during Casein Proteolysis by Curly Kale (<i>Brassica oleracea</i> L. var. <i>sabellica</i> L.) Leaf Extract: An In Silico Preliminary Study
title_short Potential Biological Activities of Peptides Generated during Casein Proteolysis by Curly Kale (<i>Brassica oleracea</i> L. var. <i>sabellica</i> L.) Leaf Extract: An In Silico Preliminary Study
title_full Potential Biological Activities of Peptides Generated during Casein Proteolysis by Curly Kale (<i>Brassica oleracea</i> L. var. <i>sabellica</i> L.) Leaf Extract: An In Silico Preliminary Study
title_fullStr Potential Biological Activities of Peptides Generated during Casein Proteolysis by Curly Kale (<i>Brassica oleracea</i> L. var. <i>sabellica</i> L.) Leaf Extract: An In Silico Preliminary Study
title_full_unstemmed Potential Biological Activities of Peptides Generated during Casein Proteolysis by Curly Kale (<i>Brassica oleracea</i> L. var. <i>sabellica</i> L.) Leaf Extract: An In Silico Preliminary Study
title_sort potential biological activities of peptides generated during casein proteolysis by curly kale (<i>brassica oleracea</i> l. var. <i>sabellica</i> l.) leaf extract: an in silico preliminary study
publisher MDPI AG
publishDate 2021
url https://doaj.org/article/d90175ff77864d5ab3e30ebf458ed064
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