Abstract: On the basis of fungus-inhibitory activity tested with dual culture method, authors studied characteristics of β-glucanase produced by B. velezensis YB15. Results showed that the strain played an antagonistic role against many pathogenic fungi. Width of inhibition zone against Helicobasidium purpureum was 11.0 and 10.6 mm by YB15 and its β-glucanase crude enzyme, respectively. Different inoculation methods could impose impacts on the formation of the hydrolytic transparent circle of the glucanase of YB15. The proportion of hydrolytic circle and colony diameter by dibbling could be up to 14.1 at 72 h. The cloned gene of YB15 β-glucanase named as Bglu1 was 732 bp in length and encoded 243 amino acids. The protein showed high homology with β-1,3-1,4-glucanase of B. amyloliquefaciens TB2 belonging to glycosyl hydrolase-16 family. The N-terminal hydrophobic domain had signal peptide and transmembrance domain.