Biochemical Characterization of Elastase From Pseudomonas aeruginosa SES 938-1

Authors : Semra KOCABIYIK and Ezgi ERGİN

Pages : 181-188

View : 13 | Download : 7

Publication Date : 1998-12-01

Article Type : Research Paper

Abstract :We have investigated some biochemical properties of elastase from a new strain o f Pseudomonas aeruginosa insert ignore into journalissuearticles values(SES 938-1);. Activities were measured at 410 nm using N-succinyl-L-insert ignore into journalissuearticles values(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.
Keywords : Turk J Biol, 22, 1998, , 181 188 Turk J Biol, vol 22, iss 2