Optimization and comparative characterization of neuraminidase activities from Pseudomonas aeruginosa with Klebsiella pneumoniae, Hep-2 cell, sheep kidney and rat liver lysosome

The properties of neuraminidase produced by P. aeruginosa strain PAO1 during growth
in a defined medium (BHI) was examined and compared with some neuraminidase features of K. pneumoniae in this
investigation.
Materials and Methods: The enzyme was isolated from concentrated culture supernatants of P. aeruginosa which was used
in a sensitive fluorometric assay by using 2’-(4-methylumbelliferyl) α-D-N acetylneuraminic acid as substrate.
Results: Neuraminidase production in P. aeruginosa PAO1 paralleled bacterial growth in defined medium (BHI) and was
maximal in the late logarithmic phase of growth but decreased during the stationary phase, probably owing to protease
production or thermal instability. Highest production of P. aeruginosa PAO1 neuraminidase was in BHI culture media. The
neuraminidase of P. aeruginosa PAO1 possessed an optimum temperature of activity at 56 °C and the activity was maximal
at pH 5. Heating the enzyme to 56 °C for 45 min., in the presence of bovine serum albumin destroyed 33.1% of it’s activity
and addition of Ca+2, EDTA and NANA also decreased activity markedly.
Conclusion: The results revealed that the highest specific activity is for p. aeruginosa PAO1