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Abstract
Extracellular mannanase activity produced bySporotrichum 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°C were 30 and 9 min for M1 and M2 respectively.
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