Purification and characterization of a beta-1,3-glucanase from the novel mycoparasite Periconia byssoides.
An extracellular beta-1,3-glucanase with antifungal properties was secreted by the novel mycoparasite, Periconia byssoides. The glucanase has a molecular mass of 35 kDa estimated by SDS-PAGE. Its optimum activity was at pH 6.0 and 50 degrees C (over 2 h). The purified beta-1,3-glucanase was capable of degrading cell walls, and inhibiting mycelia growth and spore germination of plant pathogenic fungi including Fulvia fulva, Fusarium sp. and Rhizoctonia solani. The N-terminal amino acid residues of the purified beta-1,3-glucanase are LKNGGPSFGA, which do not have any homology with previously described glucanases, suggesting it may be a novel member of the fungal beta-1,3-glucanases.
Lin
Chao
C
Laboratory for Conservation and Utilization of Bio-resources, Yunnan University, Kunming, PR China.
Yang
Jinkui
J
Sun
Hui
H
Huang
Xiaowei
X
Wang
Ruibin
R
Zhang
Ke-Qin
KQ
D000935:Antifungal Agents / Q000008:administration & dosage* / Q000737:chemistry* / Q000378:metabolism; D001203:Ascomycota / Q000145:classification / Q000201:enzymology*; D005658:Fungi / Q000166:cytology* / Q000187:drug effects*; D043326:Glucan 1,3-beta-Glucosidase / Q000008:administration & dosage* / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D013045:Species Specificity
D000935:Antifungal Agents; D043326:Glucan 1,3-beta-Glucosidase