Purification and properties of pectate lyase produced by streptomyces fradiae ifo 3439

Abstract

A pectate lyase (EC 4.2.2.2) was purified from the culture filtrate of Streptomyces fradiae by precipitation with ammonium sulfate, followed by column chromatography on DEAE-Sephadex A-50, SP-Sephadex C-50 and by gel-filtration on Sephadex G-100. The enzyme was an endo-pectate lyase with an optimum activity at pH 9.09.2, and required only calcium ion for the activity. The enzyme had macerating activity and was active on both native pectin and polygalacturonic acid, but the activity toward oligogalacturonides was small. © Taylor & Francis Group, LLC.