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 9.0_??_9.2, 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.