Abstract
The antagonistic fungus Trichoderma harzianum CECT 2413 produces at least two extracellular beta-1,6-glucanases, among other hydrolases acting on polysaccharides from fungal cell walls, when grown in chitin as the sole carbon source. We have previously reported on the purification and biochemical characterization of the major activity, which corresponds to an acidic enzyme named BGN16.2 [de la Cruz, J., Pintor-Toro, J.A., Benítez, T. & Llobell, A. (1995) J. Bacteriol. 177, 1864-1871]. In this paper, we report on the purification to electrophoretical homogeneity of BGN16.1, the second beta-1, 6-glucanase enzyme. BGN16.1 was purified by ammonium sulfate precipitation followed by adsorption and digestion of pustulan (a beta-1,6-glucan), chromatofocusing and gel-filtration chromatography. BGN16.1 is a non-glycosylated protein with an apparent molecular mass of 51 kDa and a basic isoelectric point (pI 7.4-7.7). The enzyme was active toward substrates containing beta-1,6-glycosidic linkages, including yeast cell walls. The Km was 0.8 mg x mL-1 with pustulan as the substrate. Reaction product analysis by HPLC clearly indicated that BGN16.1 has an endo-hydrolytic mode of action. The probable role of this enzyme in the antagonistic action of T. harzianum is also discussed.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
