title: Purification and some properties of endopolygalacturonase from Rhizopus sp. LKN.
abstract: An endopolygalacturonase of Rhizopus sp. strain LKN, one of several isolates from tempe starter (ragi), was purified 235-fold by CM-Sephadex C-50, DEAE-Sephadex A-50 ion exchange chromatographies and Sephadex G-75 gel filtration. The purified enzyme was homogeneous by SDS-PAGE with a M r of 38.5 kDa. Its K m value for pectic acid was 2 mg/ml. It was stable at pH 4.5 to 11 and up to 50°C, with optimum activity at pH 4.5 to 4.75 and 55 to 60°C. Some ionic compounds enhanced the enzyme activity, whereas tannic acid at 0.5 mM caused about 90% inhibition.
authors.affiliation: , .
authors.forename: F B
authors.initials: FB
authors.lastname: Elegado
authors.forename: Y
authors.initials: Y
authors.lastname: Fujio