Purification and properties of a beta-1,3-glucanase from Chaetomium sp. that is involved in mycoparasitism.
A beta-1,3-glucanase was detected, using laminarin as substrate, in the culture broth of Chaetomium sp. Major activity was associated with a 70 kDa protein band visualized on a polyacrylamide gel. beta-1,3-Glucanase was purified by a one-step, native gel purification procedure. Optimal activity was observed at pH 6.0 and 30 degrees C (over 30 min). It could degrade cell walls of plant pathogens including Rhizoctonia solani, Gibberella zeae, Fusarium sp., Colletotrichum gloeosporioides and Phoma sp. The N-terminal amino acid residues of the purified beta-1,3-glucanase are PYQLQTP, which do not exhibit homology to other fungal beta-1,3-glucanases suggesting it may be a novel enzyme.
Sun
Hui
H
Laboratory for Conservation and Utilization of Bio-resources, Yunnan University, Kunming, PR China.
Yang
Jinkui
J
Lin
Chao
C
Huang
Xiaowei
X
Xing
Ruihuan
R
Zhang
Ke-Qin
KQ
D002597:Chaetomium / Q000201:enzymology* / Q000472:pathogenicity; D005656:Fungal Proteins / Q000737:chemistry / Q000302:isolation & purification*; D043326:Glucan 1,3-beta-Glucosidase / Q000737:chemistry / Q000302:isolation & purification*; D010935:Plant Diseases / Q000382:microbiology; D017386:Sequence Homology, Amino Acid
D005656:Fungal Proteins; D043326:Glucan 1,3-beta-Glucosidase