STUDIES ON THE GALACTOMANNAN-DEGRADING ENZYMES PRODUCED BY SPOROTRICHUM-CELLULOPHILUM

Extracellular mannanase activity produced by Sporotrichum cellulophilum was purified into two components using acetone precipitation, SP-Sephadex C50 ion exchange chromatography and preparative polyacrylamide gel electrophoresis. The purified mannanse components, M1 and M2, had molecular weights of 108 000-112 000 and 32 200-36 000 respectively. Component M1 was shown to contain 2 subunits having molecular weights of 62 000 and 50 000. M1 and M2 had similar pH-activity profiles with pH optima of 5.5 and 6.0 respectively. M1 was more thermostable than M2: half lives of the enzymes at 70-degrees-C were 30 and 9 min for M1 and M2 respectively.