PURIFICATION, AND CHARACTERIZATION OF A BETA-MANNANASE OF TRICHODERMA-REESEI C-30

Trichoderma reesei was studied for its ability to produce beta-mannanase activity on a variety of carbon sources. The highest beta-mannanase activity was produced on cellulose, whereas beta-mannan-containing carbon sources (such as konjac powder or locust bean gum) gave lower enzyme titres. The enzyme responsible for the major beta-mannanolytic activity from T. reesei was purified to physical homogeneity by preparative chromatofocusing and anion exchange fast protein liquid chromatography. This beta-mannanase is a glycoprotein, with a molecular mass of 46 (+/-2) kDa and an isoelectric point of 5.2. It has an optimal pH at 5.0 and broad pH stability (2.5-7.0). It is stable for 60 min at 55-degrees-C, and has an optimal temperature for activity at 75-degrees-C. During incubation with locust bean gum, the enzyme releases mainly tri- and disaccharides.