کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8500004 | 1553681 | 2015 | 11 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Proteolysis of milk proteins by AprX, an extracellular protease identified in Pseudomonas LBSA1 isolated from bulk raw milk, and implications for the stability of UHT milk
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موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش تغذیه
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
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 °C. Peptides released from purified αS1-, β- and κ-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.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: International Dairy Journal - Volume 49, October 2015, Pages 78-88
Journal: International Dairy Journal - Volume 49, October 2015, Pages 78-88
نویسندگان
A. Matéos, M. Guyard-Nicodème, F. Baglinière, J. Jardin, F. Gaucheron, A. Dary, G. Humbert, J.-L. Gaillard,