Isolation and Fundamental Properties of enofo-Pectate Lyase pI-Isozymes from Erwinia carotovora

Abstract

A strain of Erwinia carotovora was found to produce extracellularly four kinds of endo-pectate lyase pl-isozyme (PATE-I, -II, -III and -IV) having similar properties. The four pl-isozymes were purified to homogenous states by ion exchange chromatography, gel filtration and isoelectric focusing. The approximate molecular weights were 28,000 for PATE-I and -III, 32,000 for PATE-II and 33,000 for PATE-IV, respectively, and they had isoelectric points of 10 ~ 11. The optimum pHs for the reaction catalyzed by these pl-isozymes were 9.3 for PATE-II, 9.5 for PATE-IV and 9.7 for PATE-I and III, respectively. There were no differences in the optimum Ca2+ concentration (0.5~0.6mM) or Km and Vmax among these four pl-isozymes. The mode of action of all the pl-isozymes was determined to be the endo-type. © 1984, Japan Society for Bioscience, Biotechnology, and Agrochemistry. All rights reserved.