Isolation, purification and some properties of pectate lyase synthesized by Xanthomonas campestris campestris

Abstract

 Pectase lyase (PL) was isolated from Xanthomonas campestris campestris and partially purified by ammonium sulphate precipitation.  Some properties of the enzyme were determined.  The PL activity was stimulated at 20mM, 3mM, 1mM, 1mM and 0.01mM of Ca⁺⁺, Ba⁺⁺, K^+, Na⁺, Mg⁺⁺ and NH₄⁺ respectively.  Below and above 0.1mM of each of ethylenediaminetetraacetic acid (EDTA), iodoacetic acid (IAA) and 2,4-dinitrophenol (DNP), the PL activity was inhibited.  Optimum PL activity was obtained at 40°C and incubation period of 1 hour.  The enzyme was inactivated at 50mins of boiling.