Agricultural and Biological Chemistry · 1972 · 16 citations · 0 references
Life SciencesBiochemistryMicrobiologyBiocatalysisEnzymologyMicrobial MetabolismEnzyme CharacterizationEnzyme KineticsMicrobial FermentationMicrobial Physiology In FermentationPectin Hydrolysis ProductsPectinolytic ActivityPectinolytic EnzymesPectolytic Enzyme ProductionPolygalacturonase Activity
Pectolytic enzyme formation by whole cells of Erwinia aroideae was markedly stimulated when nalidixic acid was added to a culture medium. The activity of pectolytic enzyme was markedly stimulated by nalidixic acid when the activity was measured by the decrease of viscosity of pectin, while activities of both polygalacturonic acid trans-eliminase and polygalacturonase which were measured respectively by the increase of optical density at 230 nm and the liberation of aldehyde groups, were not stimulated. The analysis of pectolytic enzyme by carboxymethyl cellulose column chromatography indicated that there was a significant difference in the elution profiles between the pectolytic enzyme induced by nalidixic acid and that synthesized under normal conditions. Therefore, we conclude that two enzymes are distinct protein species.