Abstract
Abstract An X-prolyl dipeptidyl aminopeptidase was purified from Propionibacterium shermanii NCDO 853, by a combination of DEAE chromatography, hydrophobic interaction chromatography and chromatofocusing. It had an isoelectric point near pH 4.1 and a molecular mass of approximately 84 kDa, as estimated by SDS-PAGE and gel filtration. The purified enzyme had activity optima at 40 °C and pH 7. Enzyme activity was not affected by 1 mM EDTA, Ca 2+ , Mg 2+ or reducing agents like 2-mercaptoethanol, but it was inhibited by 1 mM Cu 2+ and phenylmethylsulfonyl fluoride, indicating that it is a serine enzyme.
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