Biochemical characterization and antifungal activity of an endo-1,3-beta-glucanase of Paenibacillus sp. isolated from garden soil.
A 44-kDa 1,3-beta-glucanase was purified from the culture medium of a Paenibacillus strain with a 28-fold increase in specific activity with 31% recovery. The purified enzyme preferentially catalyzes the hydrolysis of glucans with 1,3-beta-linkage and has an endolytic mode of action. The enzyme also showed binding activity to various insoluble polysaccharides including unhydrolyzable substrates such as xylan and cellulose. The antifungal activity of this Paenibacillus enzyme and a previously purified 1,3-beta-glucanase from Streptomyces sioyaensis were examined in this study. Both enzymes had the ability to damage the cell-wall structures of the growing mycelia of phytopathogenic fungi Pythium aphanidermatum and Rhizoctonic solani AG-4. Nonetheless, the Paenibacillus enzyme had a much stronger effect on inhibiting the growth of fungi tested.
Hong
T-Y
TY
Graduate Institute of Biotechnology, National Chung Hsing University, 250 Kuo-Kuang Rd, 40227 Taichung, Taiwan, ROC.
Meng
M
M
D000595:Amino Acid Sequence; D000935:Antifungal Agents / Q000737:chemistry* / Q000494:pharmacology*; D001406:Bacillaceae / Q000201:enzymology* / Q000235:genetics; D001483:Base Sequence; D004269:DNA, Bacterial / Q000235:genetics; D004275:DNA, Ribosomal / Q000235:genetics; D004693:Glucan Endo-1,3-beta-D-Glucosidase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism / Q000494:pharmacology*; D007700:Kinetics; D008826:Microbial Sensitivity Tests; D008970:Molecular Weight; D017386:Sequence Homology, Amino Acid; D012988:Soil Microbiology; D013379:Substrate Specificity
D000935:Antifungal Agents; D004269:DNA, Bacterial; D004275:DNA, Ribosomal; D004693:Glucan Endo-1,3-beta-D-Glucosidase