ISSN:
1574-6968
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Biology
Notes:
A β-1,3-glucanase, from culture filtrates of Trichoderma harzianum, was purified in sequential steps by gel filtration, hydrophobic interaction and ion exchange chromatography. A typical procedure provided 69-fold purification with 0.32% yield. The molecular mass of the protein was found to be approximately 29 kDa, as estimated by SDS-PAGE on a 10% slab gel. The KM and Vmax values for β-1,3-glucanase, using laminarin as substrate, were 1.72 mg ml−1 and 3.10 U ml−1, respectively. The pH optimum for the enzyme was pH 4.4 and maximum activity was obtained at 50°C. The enzyme was strongly inhibited by HgCl2 and SDS. These results suggest that each β-1,3-glucanase produced by T. harzianum is different and is probably encoded by different genes.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1574-6968.2000.tb08944.x
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