Hydrolysis of cheese peptides by extracellular proteinase from Pseudomonas fluorescens TR2
(EN)
Roussis, I. G.
(EN)
Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας
(EL)
Roussis, I. G.
(EN)
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.
(EN)