{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Deracinois B"],"funding":["Région Hauts-de-France","ANR","C.P.E.R"],"pagination":["2134"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8471704"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["10(9)"],"pubmed_abstract":["The identification of phosphopeptides is currently a challenge when they are part of a complex matrix of peptides, such as a milk protein enzymatic hydrolysate. This challenge increases with both the number of phosphorylation sites on the phosphopeptides and their amino acid length. Here, this paper reports a four-phase strategy from an enzymatic casein hydrolysate before a mass spectrometry analysis in order to enhance the identification of phosphopeptides and phosphosites: (i) the control protein hydrolysate, (ii) a two-step enzymatic dephosphorylation of the latter, allowing for the almost total dephosphorylation of peptides, (iii) a one-step enzymatic dephosphorylation, allowing for the partial dephosphorylation of the peptides and (iv) an additional endoGluC enzymatic hydrolysis, allo"],"journal":["Foods (Basel, Switzerland)"],"pubmed_title":["Partial-, Double-Enzymatic Dephosphorylation and EndoGluC Hydrolysis as an Original Approach to Enhancing Identification of Casein Phosphopeptides (CPPs) by Mass Spectrometry."],"pmcid":["PMC8471704"],"funding_grant_id":["Alibiotech","AllInPep","ANR-11- EQPX-0037"],"pubmed_authors":["Deracinois B","Boulier A","Flahaut C","Romelard A","Ravallec R","Baniel A","Mateos A","Auger J"],"additional_accession":[]},"is_claimable":false,"name":"Partial-, Double-Enzymatic Dephosphorylation and EndoGluC Hydrolysis as an Original Approach to Enhancing Identification of Casein Phosphopeptides (CPPs) by Mass Spectrometry.","description":"The identification of phosphopeptides is currently a challenge when they are part of a complex matrix of peptides, such as a milk protein enzymatic hydrolysate. This challenge increases with both the number of phosphorylation sites on the phosphopeptides and their amino acid length. Here, this paper reports a four-phase strategy from an enzymatic casein hydrolysate before a mass spectrometry analysis in order to enhance the identification of phosphopeptides and phosphosites: (i) the control protein hydrolysate, (ii) a two-step enzymatic dephosphorylation of the latter, allowing for the almost total dephosphorylation of peptides, (iii) a one-step enzymatic dephosphorylation, allowing for the partial dephosphorylation of the peptides and (iv) an additional endoGluC enzymatic hydrolysis, allo","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Sep","modification":"2026-05-01T03:10:28.689Z","creation":"2022-02-11T11:28:51.528Z"},"accession":"S-EPMC8471704","cross_references":{"pubmed":["34574245"],"doi":["10.3390/foods10092134"]}}