title: Optimization and comparative characterization of neuraminidase activities from Pseudomonas aeruginosa with Klebsiella pneumoniae, Hep-2 cell, sheep kidney and rat liver lysosome.
abstract: OBJECTIVE
  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.
  
  
  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.
  
  
  CONCLUSIONS
  The results revealed that the highest specific activity is for p. aeruginosa PAO1.
authors.affiliation: Department of Microbiology, Faculty of Veterinary Medicine, University of Urmia, Urmia, Iran.
authors.forename: C
authors.initials: C
authors.lastname: Ghazaei
authors.forename: M
authors.initials: M
authors.lastname: Ahmadi
authors.forename: N
authors.initials: N
authors.lastname: Hosseini Jazani