Analysing para-κ-casein and related peptides as indicators of milk proteolysis
A new capillary electrophoresis (CE) method was used to analyse raw, pasteurised and UHT milk samples. Some para-κ-casein-related peaks were observed in raw and pasteurised milks stored at 6°C for 5 or more days, and in UHT milks stored at 20°C for 30, 60 or 90 d. The presence of these peaks was attributed to the action of proteases from psychrotrophic bacteria on κ-casein. In the CE analysis, the area of pure κ-casein digested with a proteinase-containing cell-free extract from Pseudomonas fluorescens B52 was gradually reduced and several peaks with migration times close to para-κ-casein like those found in the stored milks, appeared. On the other hand, in the sample of κ-casein treated with chymosin, only one peak corresponding to para-κ-casein was formed. The analysis of the tryptic digests of these samples by high performance liquid chromatography (HPLC) coupled to electrospray mass spectrometry (ES-MS) revealed the presence of fragments 1-105, 1-103, 1-104, 1-106 and 1-107 of κ-casein (para-κ-casein and other related peptides) in the sample of this protein treated with the P. fluorescens B52 proteinase. Their separation by CE permits them to be used as indicators of proteolysis in the casein fraction of milks.
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AVA Agrar-Verlag Allgäu
2003
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dig-cial-es-10261-2565332022-01-31T17:13:27Z Analysing para-κ-casein and related peptides as indicators of milk proteolysis Miralles, Beatriz Amigo, Lourdes Ramos, Mercedes Recio, Isidra A new capillary electrophoresis (CE) method was used to analyse raw, pasteurised and UHT milk samples. Some para-κ-casein-related peaks were observed in raw and pasteurised milks stored at 6°C for 5 or more days, and in UHT milks stored at 20°C for 30, 60 or 90 d. The presence of these peaks was attributed to the action of proteases from psychrotrophic bacteria on κ-casein. In the CE analysis, the area of pure κ-casein digested with a proteinase-containing cell-free extract from Pseudomonas fluorescens B52 was gradually reduced and several peaks with migration times close to para-κ-casein like those found in the stored milks, appeared. On the other hand, in the sample of κ-casein treated with chymosin, only one peak corresponding to para-κ-casein was formed. The analysis of the tryptic digests of these samples by high performance liquid chromatography (HPLC) coupled to electrospray mass spectrometry (ES-MS) revealed the presence of fragments 1-105, 1-103, 1-104, 1-106 and 1-107 of κ-casein (para-κ-casein and other related peptides) in the sample of this protein treated with the P. fluorescens B52 proteinase. Their separation by CE permits them to be used as indicators of proteolysis in the casein fraction of milks. 2021-12-20T13:00:11Z 2021-12-20T13:00:11Z 2003 2021-12-20T13:00:12Z artículo http://purl.org/coar/resource_type/c_6501 issn: 0026-3788 Milchwissenschaft 58(7-8): 412-415 (2003) http://hdl.handle.net/10261/256533 Sí none AVA Agrar-Verlag Allgäu |
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A new capillary electrophoresis (CE) method was used to analyse raw, pasteurised and UHT milk samples. Some para-κ-casein-related peaks were observed in raw and pasteurised milks stored at 6°C for 5 or more days, and in UHT milks stored at 20°C for 30, 60 or 90 d. The presence of these peaks was attributed to the action of proteases from psychrotrophic bacteria on κ-casein. In the CE analysis, the area of pure κ-casein digested with a proteinase-containing cell-free extract from Pseudomonas fluorescens B52 was gradually reduced and several peaks with migration times close to para-κ-casein like those found in the stored milks, appeared. On the other hand, in the sample of κ-casein treated with chymosin, only one peak corresponding to para-κ-casein was formed. The analysis of the tryptic digests of these samples by high performance liquid chromatography (HPLC) coupled to electrospray mass spectrometry (ES-MS) revealed the presence of fragments 1-105, 1-103, 1-104, 1-106 and 1-107 of κ-casein (para-κ-casein and other related peptides) in the sample of this protein treated with the P. fluorescens B52 proteinase. Their separation by CE permits them to be used as indicators of proteolysis in the casein fraction of milks. |
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artículo |
author |
Miralles, Beatriz Amigo, Lourdes Ramos, Mercedes Recio, Isidra |
spellingShingle |
Miralles, Beatriz Amigo, Lourdes Ramos, Mercedes Recio, Isidra Analysing para-κ-casein and related peptides as indicators of milk proteolysis |
author_facet |
Miralles, Beatriz Amigo, Lourdes Ramos, Mercedes Recio, Isidra |
author_sort |
Miralles, Beatriz |
title |
Analysing para-κ-casein and related peptides as indicators of milk proteolysis |
title_short |
Analysing para-κ-casein and related peptides as indicators of milk proteolysis |
title_full |
Analysing para-κ-casein and related peptides as indicators of milk proteolysis |
title_fullStr |
Analysing para-κ-casein and related peptides as indicators of milk proteolysis |
title_full_unstemmed |
Analysing para-κ-casein and related peptides as indicators of milk proteolysis |
title_sort |
analysing para-κ-casein and related peptides as indicators of milk proteolysis |
publisher |
AVA Agrar-Verlag Allgäu |
publishDate |
2003 |
url |
http://hdl.handle.net/10261/256533 |
work_keys_str_mv |
AT mirallesbeatriz analysingparakcaseinandrelatedpeptidesasindicatorsofmilkproteolysis AT amigolourdes analysingparakcaseinandrelatedpeptidesasindicatorsofmilkproteolysis AT ramosmercedes analysingparakcaseinandrelatedpeptidesasindicatorsofmilkproteolysis AT recioisidra analysingparakcaseinandrelatedpeptidesasindicatorsofmilkproteolysis |
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1777671513511559168 |