Biochemical Characterization of Elastase From Pseudomonas aeruginosa SES 938-1

Authors: Semra KOCABIYIK, Ezgi ERGİN

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.

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