Journals / Turkish Journal of Biology / 1998 / Cilt: 22 - Sayı: 2
Biochemical Characterization of Elastase From Pseudomonas aeruginosa SES 938-1
- Journal
- Turkish Journal of Biology
- Pages
- 181–188
- DOI
- —
Abstract
We have investigated some biochemical properties of elastase from a new strain o f Pseudomonas aeruginosa (SES 938-1). Activities were measured at 410 nm using N-succinyl-L-(ala) 3 -p- nitroanilide as substrate. The elastase activity followed Michaelis-Menten kinetics over the substrate range of 0.067-0.540 mM with the apparent K m value of 0.375 mM. Optimum activity was observed at 36 °C and pH 7.5. elastase activity was inhibited by metal chelating agents and high concentrations of Mn 2+ , Zn 2+ and Ni 2+ . The results obtained suggest that elastase from P. aeruginosa SES 938-1 is a neutral metalloproteinase.
Özet
We have investigated some biochemical properties of elastase from a new strain o f Pseudomonas aeruginosa (SES 938-1). Activities were measured at 410 nm using N-succinyl-L-(ala) 3 -p- nitroanilide as substrate. The elastase activity followed Michaelis-Menten kinetics over the substrate range of 0.067-0.540 mM with the apparent K m value of 0.375 mM. Optimum activity was observed at 36 °C and pH 7.5. elastase activity was inhibited by metal chelating agents and high concentrations of Mn 2+ , Zn 2+ and Ni 2+ . The results obtained suggest that elastase from P. aeruginosa SES 938-1 is a neutral metalloproteinase.