Abstract
A β-1,3-glucanase was detected, using laminarin as substrate, in the culture broth of Chaetomium sp. Major activity was associated with a 70 kDa protein band visualized on a polyacrylamide gel. β-1,3-Glucanase was purified by a one-step, native gel purification procedure. Optimal activity was observed at pH 6.0 and 30 °C (over 30 min). It could degrade cell walls of plant pathogens including Rhizoctonia solani, Gibberella zeae, Fusarium sp., Colletotrichum gloeosporioides and Phoma sp. The N-terminal amino acid residues of the purified β-1,3-glucanase are PYQLQTP, which do not exhibit homology to other fungal β-1,3-glucanases suggesting it may be a novel enzyme.
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Received 20 July 2005; Revisions requested 2 August 2005 and 27 September 2005; Revisions received 16 September 2005 and 3 November 2005; Accepted 6 November 2005
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Sun, H., Yang, J., Lin, C. et al. Purification and Properties of a β-1,3-glucanase from Chaetomium sp. that is Involved in Mycoparasitism. Biotechnol Lett 28, 131–135 (2006). https://doi.org/10.1007/s10529-005-5132-0
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DOI: https://doi.org/10.1007/s10529-005-5132-0