Purification and properties of a 1,3-beta-glucanase from Penicillium oxalicum autolysates.
Purification and properties of a 1,3-beta-glucanase from Penicillium oxalicum autolysates.
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草酸青霉自溶物中 1,3-β-葡聚糖酶的纯化和性质。
DOI：
10.1111/j.1574-6968.1989.tb03675.x
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发表时间：
1989
影响因子：
2.1
通讯作者：
M. Pérez
中科院分区：
文献类型：
--
作者：
J. Copa;F. Reyes;M. Pérez
在含有草酸青霉的培养基中，1，3-β-葡聚糖酶在自溶过程中被检测到高活性。这是由于四种酶的共同作用。主要酶的纯化过程在SDS聚丙烯酰胺凝胶中产生了一条均一的条带，其相对分子质量为79,400道尔顿。该酶的等电点为6.3，仅对1，3-β-葡聚糖有活性，对海带多糖的S0.5为0.23mgml-1。该酶的最适pH为4，最适温度为55℃，当pH和温度改变时，酶的不稳定性明显。该酶对氧化的海带多糖没有活性，且几乎不受葡聚糖-D-内酯的抑制。Hg2+、Ag+和Fe2+是有效的抑制剂。该酶被刀豆蛋白-A-琼脂糖吸附。
High 1,3-beta-glucanase activity was detected during autolysis in a culture medium containing Penicillium oxalicum. It was due to the combined action of four enzymes. The purification process for the major enzyme produced a homogeneous band in the SDS polyacrylamide gel that corresponded to a molecular weight of 79,400 daltons. The enzyme pI was 6.3 and it was only active against 1,3-beta-glucans, with a S0.5 of 0.23 mg ml-1 against laminarin. The enzymatic optima were found at pH 4 and 55 degrees C, and instability was evident when pH and temperature were altered. The enzyme was not active against oxidated laminarin and was barely inhibited by glucono-D-lactone. Hg2+, Ag+ and Fe2+ were effective inhibitors. The enzyme was adsorbed by concanavalin-A-sepharose.