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BGN16.3, a novel acidic β‐1,6‐glucanase from mycoparasitic fungus Trichoderma harzianum CECT 2413
Author(s) -
Montero Manuel,
Sanz Luis,
Rey Manuel,
Monte Enrique,
Llobell Antonio
Publication year - 2005
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2005.04762.x
Subject(s) - trichoderma harzianum , glucanase , fungus , trichoderma , botany , chemistry , biology , enzyme , organic chemistry , biological pest control
A new component of the β‐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‐β‐1,6‐glucanase activity described up to now in T. harzianum CECT 2413. BGN16.3 is an acidic β‐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 β‐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 β‐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 β‐1,6‐glucanases in this process is discussed.