Studies on the Protopectinase Produced by Verticillium sp. (Part 2) Purification and Properties of Protopectinase from Verticillium sp.

Verticillium sp. 가 생산하는 Protopectin 용해효소에 관한 연구 (제 2 보) 효소의 정제 및 성질

The protopectinase from the culture extract of a Verticillium sp. was purified about 1000 fold by ammonium sulfate fractionation, DEAE-Sephadex treatment and Sephadex G-75 column chromatography. The purified enzyme was homogeneous on electrophoresis and its molecular weight was estimated to be 38000 by Andrew's gel filtration, method. The enzyme was almost stable under the temperature of 4$0^{\circ}C$ and within the pH range of 3-5. Its optimum pH and temperature were 4 and 4$0^{\circ}C$, respectively. The activity was markedly inhibited by galacturonic acid. The purified enzyme was able to macerate various kinds of plant tissues, such as radish, cucumber, onion, carrot, and potato. It also reduced the viscosity of pectin solution more rapidly than that of pectic acid solution and showed no lyase or CMCase activity.