Armillariella tabescens EJLY2098 β-甘露聚糖酶atMAN47的纯化及酶学性质分析

以魔芋精粉为唯一碳源, 对假蜜环菌(Armillariella tabescens) EJLY2098进行培养, 诱导其产生β-甘露聚糖酶。经DEAE－阴离子交换层析后, 分离纯化出β-甘露聚糖酶atMAN47。酶学性质分析: 该酶分子量约为47 kD, 酶的最适反应温度为50°C, 在pH 5.0~6.5之间该酶的稳定性较好; Na+ 和Ba2+ 对该酶有激活作用, 用TLC对酶产物分析, 表明该酶为内切β-甘露聚糖酶。该酶为偏酸性的内切甘露聚糖酶, 适合发展为饲料的酶制剂, 具有良好的应用前景。

Purification and Characterization of β-mannanase atMAN47 from Armillariella tabescens

Armillariella tabescens EJLY2098 was induced to produce β-mannanase with konjac fine flour (Amorphopallus rivieri) as single carbon source. This induced enzyme was then purified using DEAE ion exchange chromatography and named atMAN47. Zymologic analysis showed that the molecular weight of this P-mannanase was approximately 47 kD. The enzyme was stable when pH ranged from 5.0 to 6.5 and could be activated by Na~+ and Ba~(2+). With an optimal temperature of 50℃. Action mode analysis of TLC re-vealed that the enzyme belonged to the endo-P-mannanase family. Being a meta-acid endo-β-mannanase, it was suitable to be applied to feed industry with a promising future as an enzyme preparation.