Khowala S, Sengupta S
Arch Biochem Biophys. 1985 Sep;241(2):533-9. doi: 10.1016/0003-9861(85)90578-8.
The enzyme, endo-alpha-mannanase, from culture filtrate of a mushroom Volvariella volvacea has been purified 73-fold by acetone precipitation, ion-exchange chromatography (DEAE-Sephadex), and gel-permeation chromatographies on Bio-Gel P-300 and on Sephacryl S-200 columns. The enzyme preparation gave a single protein band on sodium dodecyl sulfate-disc gel electrophoresis at pH 6.8 and has a molecular weight of approx. 56,000. It has no alpha- or beta-mannosidase activity and does not act on beta-gluco-or galactomannan. The enzyme shows maximum activity on baker's yeast alpha-mannan at pH 5.0 and at 55 degrees C, and is fairly stable between pH 3 and 6 and temperatures up to 50 degrees C. The Km is 32.25 mg mannan/ml. Enzyme activity is inhibited by Hg2+, sodium azide, iodoacetic acid, EDTA, and Ag+, in decreasing order.
从草菇培养滤液中提取的内切α-甘露聚糖酶，通过丙酮沉淀、离子交换色谱法（DEAE-葡聚糖凝胶）以及在Bio-Gel P-300和Sephacryl S-200柱上的凝胶渗透色谱法进行纯化，纯化倍数达73倍。该酶制剂在pH 6.8的十二烷基硫酸钠圆盘凝胶电泳上呈现单一蛋白条带，分子量约为56,000。它没有α-或β-甘露糖苷酶活性，且不作用于β-葡聚糖或半乳甘露聚糖。该酶在pH 5.0和55℃时对面包酵母α-甘露聚糖表现出最大活性，在pH 3至6以及温度高达50℃之间相当稳定。Km为32.25 mg甘露聚糖/毫升。酶活性按递减顺序受到Hg2 +、叠氮化钠、碘乙酸、EDTA和Ag +的抑制。
