Hydrolysis of cheese peptides by extracellular proteinase from Pseudomonas fluorescens TR2
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Date
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Roussis, I. G.
Alexopoulos, C.
Sakarellos-Daitsiotis, M.
Triantafyllidou, M.
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VOLKSWIRTSCHAFTLICHER VERLAG
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peer reviewed
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Milchwissenschaft-Milk Science International
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The ability of Pseudomonas fluorescens TR2 proteinase to hydrolyse cheese peptides was examined. TR2 proteinase hydrolysed peptides of cheese water soluble extract, exhibiting a preference for hydrolysis of small peptides. The main peptide produced by the action of pepsin on alpha(s1)-casein was rapidly degraded as indicated by RP-HPLC chromatography. TR2 proteinase degraded a characteristic group of hydrophobic peptides of cow cheese water soluble extract, and more rapidly a broad "hydrophobic" peak of ewe cheese extract. SDS-Page electrophoresis showed that 2 main peptides of both cow and ewe extracts of about 18 and 14 KDa were not degraded by TR2 proteinase. TR2 proteinase did not exhibit aminopeptidase activity.
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Keywords
pseudomonas fluorescens (extracellular proteinase)
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<Go to ISI>://000086615300008
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en
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Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας