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首页> 外文期刊>Journal of Biotechnology >Softwood hemicellulose-degrading enzymes from Aspergillus niger:Purification and properties of a beta-mannanase
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Softwood hemicellulose-degrading enzymes from Aspergillus niger:Purification and properties of a beta-mannanase

机译：来自Aspergillus尼日尔的软木半纤维素降解酶：β-甘露糖酶的纯化和性质

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摘要

The enzymes needed for galactomannan hydrolysis, i.e. beta-mannanase, alpha-galactosidase and beta-mannosidase, were produced by the filamentous fungus Aspergillus niger. The beta-mannanase was purified to electrophoretic homogeneity in three steps using ammonium sulfate precipitation, anion-exchange chromatography and gel filtration. The purified enzyme had an isoelectric point of 3.7 and a molecular mass of 40 kDa. Ivory nut mannan was degraded mainly to mannobiose and mannotriose when incubated with the beta-mannanase. Analysis by H-1 NMR spectroscopy during hydrolysis of mannopentaose showed that the enzyme acts by the retaining mechanism. The N-terminus of the purified A. niger beta-mannanase was sequenced by Edman degradation, and comparison with Aspergillus aculeatus beta-mannanase indicated high identity. The enzyme most probably lacks a cellulose binding domain since it was unable to adsorb on cellulose.
机译：通过丝状真菌曲霉产生，β-甘露聚糖酶，即β-甘露糖酶，α-半乳糖苷酶和β-甘露糖苷酶所需的酶。 使用硫酸铵沉淀，阴离子交换色谱和凝胶过滤，在三个步骤中纯化β-甘醇酶以电泳均匀性。 纯化的酶的等电点为3.7，分子量为40kDa。 与β-甘露糖酶孵育时，象牙螺母甘露甘露甘露植物主要用于甘露糖和甘露糖。 H-1 NMR光谱在水解过程中的分析表明该酶通过保持机构作用。 纯化的A.尼日尔β-甘露糖酶的N-末端被Edman降解测序，与Aspergillus Aculeatusβ-甘露糖酶的比较表明了高度的高度。 酶最可能缺乏纤维素结合结构域，因为它不能吸附在纤维素上。

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