Hong T-Y, Meng M
Graduate Institute of Biotechnology, National Chung Hsing University, 250 Kuo-Kuang Rd, 40227 Taichung, Taiwan, ROC.
Appl Microbiol Biotechnol. 2003 Jun;61(5-6):472-8. doi: 10.1007/s00253-003-1249-z. Epub 2003 Feb 25.
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.
从一株芽孢杆菌的培养基中纯化出一种44 kDa的1,3-β-葡聚糖酶，比活性提高了28倍，回收率为31%。纯化后的酶优先催化具有1,3-β-连接的葡聚糖的水解，具有内切作用模式。该酶还对包括木聚糖和纤维素等不可水解底物在内的各种不溶性多糖表现出结合活性。本研究检测了这种芽孢杆菌酶和先前从岛链霉菌中纯化的1,3-β-葡聚糖酶的抗真菌活性。两种酶都有能力破坏植物病原真菌瓜果腐霉和立枯丝核菌AG-4生长菌丝体的细胞壁结构。尽管如此，但芽孢杆菌酶对所测试真菌生长的抑制作用要强得多。
