Abstract
We purified and characterized a cold-active polygalacturonase (PG) from the extracellular fraction of Cystofilobasidium capitatum strain PPY-1. The purified PG from strain PPY-1 has a molecular mass of about 44 kDa, and exhibited high activity at 0 °C, although its optimum temperature was 45 °C. Although the Km value for polygalacturonate as a substrate at 45 °C was found to be 11.2 mg/ml, it decreased gradually with decreasing temperature, and it was 0.66 mg/ml at 0 °C. Moreover, its cleavage pattern was of the endo-type. These findings might indicate that PG from strain PPY-1 is a novel type of cold-active endo-PG that is able to degrade pectin compounds at low temperatures.