Optimization and comparative characterization of neuraminidase activities from Pseudomonas aeruginosa with Klebsiella pneumoniae,Hep-2 cell, sheep kidney and rat liver lysosome
Background and Objectives: 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...
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| Format: | Article |
| Language: | English |
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Tehran University of Medical Sciences
2010-03-01
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| Series: | Iranian Journal of Microbiology |
| Subjects: | |
| Online Access: | https://ijm.tums.ac.ir/index.php/ijm/article/view/45 |
| _version_ | 1819103705273729024 |
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| author | C Ghazaei M Ahmadi N Hosseini Jazani |
| author_facet | C Ghazaei M Ahmadi N Hosseini Jazani |
| author_sort | C Ghazaei |
| collection | DOAJ |
| description | Background and Objectives: 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. |
| first_indexed | 2024-12-22T01:54:42Z |
| format | Article |
| id | doaj.art-8ba69cb334f74472a9f211e5731c4634 |
| institution | Directory Open Access Journal |
| issn | 2008-3289 2008-4447 |
| language | English |
| last_indexed | 2024-12-22T01:54:42Z |
| publishDate | 2010-03-01 |
| publisher | Tehran University of Medical Sciences |
| record_format | Article |
| series | Iranian Journal of Microbiology |
| spelling | doaj.art-8ba69cb334f74472a9f211e5731c46342022-12-21T18:42:49ZengTehran University of Medical SciencesIranian Journal of Microbiology2008-32892008-44472010-03-0121Optimization and comparative characterization of neuraminidase activities from Pseudomonas aeruginosa with Klebsiella pneumoniae,Hep-2 cell, sheep kidney and rat liver lysosomeC Ghazaei0M Ahmadi1N Hosseini Jazani2Department of Microbiology, Faculty of Veterinary Medicine, University of Urmia, Urmia, Iran.Department of Microbiology, Faculty of Veterinary Medicine, University of Urmia, Urmia, Iran.2Department of Microbiology, Immunology and Genetics, Faculty of Medicine, Urmia University of Medical Sciences, Urmia, Iran.Background and Objectives: 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.https://ijm.tums.ac.ir/index.php/ijm/article/view/45K. pnumoniaeP. aeruginosa PAO1Neuraminidasefluorometric assayspecific activityIran |
| spellingShingle | C Ghazaei M Ahmadi N Hosseini Jazani Optimization and comparative characterization of neuraminidase activities from Pseudomonas aeruginosa with Klebsiella pneumoniae,Hep-2 cell, sheep kidney and rat liver lysosome Iranian Journal of Microbiology K. pnumoniae P. aeruginosa PAO1 Neuraminidase fluorometric assay specific activity Iran |
| title | Optimization and comparative characterization of neuraminidase activities from Pseudomonas aeruginosa with Klebsiella pneumoniae,Hep-2 cell, sheep kidney and rat liver lysosome |
| title_full | Optimization and comparative characterization of neuraminidase activities from Pseudomonas aeruginosa with Klebsiella pneumoniae,Hep-2 cell, sheep kidney and rat liver lysosome |
| title_fullStr | Optimization and comparative characterization of neuraminidase activities from Pseudomonas aeruginosa with Klebsiella pneumoniae,Hep-2 cell, sheep kidney and rat liver lysosome |
| title_full_unstemmed | Optimization and comparative characterization of neuraminidase activities from Pseudomonas aeruginosa with Klebsiella pneumoniae,Hep-2 cell, sheep kidney and rat liver lysosome |
| title_short | Optimization and comparative characterization of neuraminidase activities from Pseudomonas aeruginosa with Klebsiella pneumoniae,Hep-2 cell, sheep kidney and rat liver lysosome |
| title_sort | optimization and comparative characterization of neuraminidase activities from pseudomonas aeruginosa with klebsiella pneumoniae hep 2 cell sheep kidney and rat liver lysosome |
| topic | K. pnumoniae P. aeruginosa PAO1 Neuraminidase fluorometric assay specific activity Iran |
| url | https://ijm.tums.ac.ir/index.php/ijm/article/view/45 |
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