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J. Bacteriol., Apr 1995, 1864-1871, Vol 177, No. 7
J de la Cruz, JA Pintor-Toro, T Benitez and A Llobell
The enzymes from Trichoderma species that degrade fungal cell walls have
been suggested to play an important role in mycoparasitic action against
fungal plant pathogens. The mycoparasite Trichoderma harzianum produces at
least two extracellular beta-1,6-glucanases, among other hydrolases, when
it is grown on chitin as the sole carbon source. One of these extracellular
enzymes was purified to homogeneity after adsorption to its substrate,
pustulan, chromatofocusing, and, finally, gel filtration. The apparent
molecular mass was 43,000, and the isoelectric point was 5.8. The first 15
amino acids from the N terminus of the purified protein have been
sequenced. The enzyme was specific for beta-1,6 linkages and showed an
endolytic mode of action on pustulan. Further characterization indicated
that the enzyme by itself releases soluble sugars and produces hydrolytic
halli on yeast cell walls. When combined with other T. harzianum cell
wall-degrading enzymes such as beta-1,3-glucanases and chitinases, it
hydrolyzes filamentous fungal cell walls. The enzyme acts cooperatively
with the latter enzymes, inhibiting the growth of the fungi tested.
Antibodies against the purified protein also indicated that the two
identified beta-1,6-glucanases are not immunologically related and are
probably encoded by two different genes.
Copyright © 1995, American Society for Microbiology
Purification and characterization of an endo-beta-1,6-glucanase from Trichoderma harzianum that is related to its mycoparasitism
Instituto de Bioquimica Vegetal y Fotosintesis, Facultad de Biologia, Universidad de Sevilla, Spain.
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