关于南比新丝核菌细胞外氧化酶的底物特异性和某些特性的研究

O. Mogilnaya, N. Ronzhin, E. Posokhina, V. Bondar
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引用次数: 0

摘要

通过用β-葡萄糖苷酶温和处理高等真菌Neonothopanus nambi的生物质,从其菌丝体中分离出了一种具有氧化酶活性的胞外酶。本研究对分离出的胞外氧化酶的底物特异性和一些特性进行了研究。实验表明,细胞外氧化酶对大多数被选为模型底物的酚类化合物具有活性。值得注意的是,在不添加外源过氧化氢和其他介质的情况下,该酶在反应中表现出催化功能。该酶对藜芦醇和二氢酚、对苯二酚和愈创木酚的催化活性最高。该酶对芳香偶氮化合物(ABTS、DAB、邻二苯胺)的活性较低。在与二水苯酚间苯二酚和一苯酚反应时,酶的效率极低。测定了酶与活性氧化底物反应的动力学参数。添加二价金属离子螯合剂(EDTA)不会影响酶的活性,而添加 SH 试剂(DTT)则会提高所研究氧化酶的催化效率。所获得的全部数据表明,在微酸性和中性条件下,南布真菌的胞外氧化酶可催化多种芳香族化合物的氧化,而无需添加额外的介质(特别是过氧化氢)。这为研究这种酶在生物医学分析中的适用性创造了先决条件。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
ON THE SUBSTRATE SPECIFICITY AND SOME PROPERTIES OF THE EXTRACELLULAR OXIDASE FROM THE NEONOTHOPANUS NAMBI BASIDIOMYCETE
An extracellular enzyme with oxidase activity was isolated from the mycelium of the higher fungus Neonothopanus nambi by mild treatment of the biomass with β-glucosidase. A substrate specificity and some properties of the isolated extracellular oxidase were studied in the present work. Experiments revealed that the extracellular oxidase exhibited activity with most phenolic compounds chosen as model substrates. It is important to note that the enzyme exhibited a catalytic function in the reactions without the addition of exogenous hydrogen peroxide and other mediators. The highest catalytic activity of the enzyme was observed with veratryl alcohol and dihydric phenols, hydroquinone and guaiacol. The enzyme showed lower activity with aromatic azo compounds (ABTS, DAB, o-dianisidine). In reactions with dihydric phenol resorcinol and monophenol, the enzyme efficiency was extremely low. The kinetic parameters of the enzymatic reactions with actively oxidized substrates were determined. The addition of a divalent metal ion chelator (EDTA) did not affect the activity of the enzyme, while the addition of the SH reagent (DTT) increased the catalytic efficiency of the studied oxidase. The totality of the data obtained indicates that the extracellular oxidase of the N. nambi fungus catalyzes the oxidation of a wide range of aromatic compounds under slightly acidic and neutral conditions without the addition of additional mediators (in particular, hydrogen peroxide). This creates the prerequisites for studying the applicability of the enzyme in biomedical analytics.
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