Abstract
Trichoderma reesei was studied for its ability to produce β-mannanase activity on a variety of carbon sources. The highest β-mannanase activity was produced on cellulose, whereas β-mannan-containing carbon sources (such as kojac powder or locust bean gum) gave lower enzyme titres. The enzyme responsible for the major β-mannanolytic activity from T. reesei was purified to physical homogeneity by preparative chromatofocusing and anion exchange fast protein liquid chromatography. This β-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° C, and has an optimal temperature for activity at 75° C. During incubation with locust bean gum, the enzyme releases mainly tri- and disaccharides.
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Correspondence to: C. P. Kubicek
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Arisan-Atac, I., Hodits, R., Kristufek, D. et al. Purification, and characterization of a β-mannanase of Trichoderma reesei C-30. Appl Microbiol Biotechnol 39, 58–62 (1993). https://doi.org/10.1007/BF00166849
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DOI: https://doi.org/10.1007/BF00166849