{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["10(11)"],"submitter":["Polak-Berecka M"],"pubmed_abstract":["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 p"],"journal":["Foods (Basel, Switzerland)"],"pagination":["2877"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8625700"],"repository":["biostudies-literature"],"pubmed_title":["Potential Biological Activities of Peptides Generated during Casein Proteolysis by Curly Kale (Brassica oleracea L. var. sabellica L.) Leaf Extract: An In Silico Preliminary Study."],"pmcid":["PMC8625700"],"pubmed_authors":["Rachwal K","Wasko A","Michalak-Tomczyk M","Polak-Berecka M","Michalak K","Skrzypczak K"],"additional_accession":[]},"is_claimable":false,"name":"Potential Biological Activities of Peptides Generated during Casein Proteolysis by Curly Kale (Brassica oleracea L. var. sabellica 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 p","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Nov","modification":"2025-04-26T05:25:57.1Z","creation":"2022-02-11T13:34:50.246Z"},"accession":"S-EPMC8625700","cross_references":{"pubmed":["34829159"],"doi":["10.3390/foods10112877"]}}