Skip to main content

Lund University Publications

LUND UNIVERSITY LIBRARIES

Primary proteolysis studied in a cast cheese made from microfiltered milk

Larsson, M ; Zakora, M ; Dejmek, Petr LU orcid and Ardö, Y (2006) IDF International Symposium on Indigenous Enzymes in Milk In International Dairy Journal 16(6). p.623-632
Abstract
Primary proteolysis was studied in a starter-free cheese model made from microfiltered (MF) milk (19.0% casein,<0.2% whey proteins). Specificity of plasmin and chymosin activity was investigated in the pH range 5.0–6.0, by analysis of peptide composition using high-performance liquid chromatography and liquid chromatography–mass spectrometry. Hydrolysis experiments with purified caseins were performed to aid identification of peptides released by specific activities. Plasmin had no activity in cheese below pH 5.4, while its activity increased from pH 5.4 to 6.0. Chymosin activity on the Phe23–Phe24 bond of αS1-casein had an optimum pH around 5.3, while release of the bitter peptide β-casein (f193–209), effected by chymosin, was highest... (More)
Primary proteolysis was studied in a starter-free cheese model made from microfiltered (MF) milk (19.0% casein,<0.2% whey proteins). Specificity of plasmin and chymosin activity was investigated in the pH range 5.0–6.0, by analysis of peptide composition using high-performance liquid chromatography and liquid chromatography–mass spectrometry. Hydrolysis experiments with purified caseins were performed to aid identification of peptides released by specific activities. Plasmin had no activity in cheese below pH 5.4, while its activity increased from pH 5.4 to 6.0. Chymosin activity on the Phe23–Phe24 bond of αS1-casein had an optimum pH around 5.3, while release of the bitter peptide β-casein (f193–209), effected by chymosin, was highest at pH 6.0. At pH <5.3, the specificity of chymosin on αS1-casein changed, and the peptide bond Leu20–Leu21 was cleaved at an increasing rate with decreasing pH. Demineralisation of the MF retentate generally increased proteolytic activity. (Less)
Please use this url to cite or link to this publication:
author
; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
chymosin, plasmin, cheese proteolysis, LC-MS, casein peptide identification
in
International Dairy Journal
volume
16
issue
6
pages
623 - 632
publisher
Elsevier
conference name
IDF International Symposium on Indigenous Enzymes in Milk
conference location
Cork, Ireland
conference dates
2005-04-19 - 2005-04-22
external identifiers
  • wos:000237141200015
  • scopus:33645418236
ISSN
0958-6946
DOI
10.1016/j.idairyj.2005.08.012
language
English
LU publication?
yes
id
40e58832-ac33-4f89-905e-85afcfc181a5 (old id 586270)
date added to LUP
2016-04-01 16:49:54
date last changed
2023-12-06 05:09:31
@article{40e58832-ac33-4f89-905e-85afcfc181a5,
  abstract     = {{Primary proteolysis was studied in a starter-free cheese model made from microfiltered (MF) milk (19.0% casein,&lt;0.2% whey proteins). Specificity of plasmin and chymosin activity was investigated in the pH range 5.0–6.0, by analysis of peptide composition using high-performance liquid chromatography and liquid chromatography–mass spectrometry. Hydrolysis experiments with purified caseins were performed to aid identification of peptides released by specific activities. Plasmin had no activity in cheese below pH 5.4, while its activity increased from pH 5.4 to 6.0. Chymosin activity on the Phe23–Phe24 bond of αS1-casein had an optimum pH around 5.3, while release of the bitter peptide β-casein (f193–209), effected by chymosin, was highest at pH 6.0. At pH &lt;5.3, the specificity of chymosin on αS1-casein changed, and the peptide bond Leu20–Leu21 was cleaved at an increasing rate with decreasing pH. Demineralisation of the MF retentate generally increased proteolytic activity.}},
  author       = {{Larsson, M and Zakora, M and Dejmek, Petr and Ardö, Y}},
  issn         = {{0958-6946}},
  keywords     = {{chymosin; plasmin; cheese proteolysis; LC-MS; casein peptide identification}},
  language     = {{eng}},
  number       = {{6}},
  pages        = {{623--632}},
  publisher    = {{Elsevier}},
  series       = {{International Dairy Journal}},
  title        = {{Primary proteolysis studied in a cast cheese made from microfiltered milk}},
  url          = {{http://dx.doi.org/10.1016/j.idairyj.2005.08.012}},
  doi          = {{10.1016/j.idairyj.2005.08.012}},
  volume       = {{16}},
  year         = {{2006}},
}