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Título
BGN16.3, a novel acidic beta-1,6-glucanase from mycoparasitic fungus Trichoderma harzianum CECT 2413
Autor(es)
Materia
b-1,6-glucanase
Cell wall degrading enzyme
Mycoparasitism
Trichoderma
Clasificación UNESCO
2414 Microbiología
Fecha de publicación
2005-06
Editor
Wiley
Citación
Montero, M., Sanz, L., Rey, M., Monte, E., & Llobell, A. (2005). BGN16. 3, a novel acidic β‐1, 6‐glucanase from mycoparasitic fungus Trichoderma harzianum CECT 2413. The FEBS journal, 272(13), 3441-3448. doi: 10.1111/j.1742-4658.2005.04762.x.
Resumen
[EN]A new component of the beta-1,6-glucanase (EC 3.2.1.75) multienzymatic complex secreted by Trichoderma harzianum has been identified and fully characterized. The protein, namely BGN16.3, is the third isozyme displaying endo-beta-1,6-glucanase activity described up to now in T. harzianum CECT 2413. BGN16.3 is an acidic beta-1,6-glucanase that is specifically induced by the presence of fungal cell walls in T. harzianum growth media. The protein was purified to electrophoretical homogenity using its affinity to beta-1,6-glucan as first purification step, followed by chomatofocusing and gel filtration. BGN16.3 has a molecular mass of 46 kDa in SDS/PAGE and a pI of 4.5. The enzyme only showed activity against substrates with beta-1,6-glycosidic linkages, and it has an endohydrolytic mode of action as shown by HPLC analysis of the products of pustulan hydrolysis. The expression profile analysis of BGN16.3 showed a carbon source control of the accumulation of the enzyme, which is fast and strongly induced by fungal cell walls, a condition often regarded as mycoparasitic simulation. The likely involvement beta-1,6-glucanases in this process is discussed.
URI
ISSN
1742-464X
DOI
10.1111/j.1742-4658.2005.04762.x
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