Journal
INTERNATIONAL DAIRY JOURNAL
Volume 49, Issue -, Pages 78-88Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.idairyj.2015.04.008
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Funding
- CNIEL (National Interprofessional Center of the Dairy Economy)
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UHT milk made from milk contaminated by Pseudomonas LBSA1 destabilised during storage. Sedimentation of UHT milk was observed; zeta potential of casein micelles decreased, while contents of non-casein nitrogen and non-protein nitrogen increased. Pseudomonas LBSA1 produced an extracellular protease that hydrolysed caseins but not whey proteins; this was identified as AprX, a thermoresistant protease belonging to the serralysin family. This protease showed a broad range of pH activity (pH 6 to pH 10) and an optimal temperature of activity of 40 degrees C. Peptides released from purified alpha(S1)-, beta- and kappa-caseins were determined by tandem mass spectrometry. The identified cleavage sites did not reveal a strong specificity of the extracellular protease. However, the presence of basic or aromatic amino acid residues in the P1 position had a positive influence on cleavage in comparison with acidic amino acid residues or proline. (C) 2015 Elsevier Ltd. All rights reserved.
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