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  • Title: Purification and characterisation of an intracellular X-prolyl-dipeptidyl aminopeptidase from Streptococcus thermophilus ACA-DC 4.
    Author: Tsakalidou E, Anastasiou R, Papadimitriou K, Manolopoulou E, Kalantzopoulos G.
    Journal: J Biotechnol; 1997 Jan 03; 59(3):203-11. PubMed ID: 9519481.
    Abstract:
    An intracellular X-prolyl-dipeptidyl aminopeptidase from Streptococcus thermophilus ACA-DC 4, isolated from traditional Greek yoghurt, was purified by anion exchange and gel filtration chromatography. A single band of molecular weight of about 80,000 appeared in SDS-PAGE; by gel filtration it was shown that the native enzyme was dimeric. The peptidase showed optimum activity on glycyl-prolyl 4-nitroanilide at pH 7.0 and at 50 degrees C, with K(m) = 3.1 mM and Vmax = 3500 U mg-1; over 50 degrees C the enzyme activity declined rapidly. It was inactivated by PMSF; sulfhydryl group reagents and metal chelators had little effect on enzyme activity.
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