来自白腐真菌粉状孢霉的纤维二糖氧化酶的一些特性。
Some properties of cellobiose oxidase from the white-rot fungus Sporotrichum pulverulentum.
作者信息
Morpeth F F
出版信息
Biochem J. 1985 Jun 15;228(3):557-64. doi: 10.1042/bj2280557.
Abstract
Cellobiose oxidase from the white-rot fungus Sporotrichum pulverulentum has been purified to homogeneity by a new procedure. The carbohydrate and amino acid compositions of the enzyme have been determined. Cellobiose oxidase contains FAD and cytochrome b prosthetic groups. Mr of the enzyme has been estimated at 74400 by sedimentation equilibrium. The enzyme is a monomer. Optical, fluorescence and e.p.r. spectra of oxidized and reduced cellobiose oxidase have been determined. A preliminary investigation of the substrate specificity of cellobiose oxidase reveals that disaccharides and even some insoluble polysaccharides are substrates, but not monosaccharides. Strong substrate inhibition is seen at high concentrations of cellobiose. This effect is particularly marked when oxygen is the electron acceptor. Cellobiose oxidase is unusual among flavoproteins, since it stabilizes the red anionic flavin semiquinone and forms a sulphite adduct, yet appears to produce the superoxide anion as its primary reduced oxygen product.
摘要
采用一种新方法已将来自白腐真菌粉状孢霉的纤维二糖氧化酶纯化至同质。已测定了该酶的碳水化合物和氨基酸组成。纤维二糖氧化酶含有黄素腺嘌呤二核苷酸（FAD）和细胞色素b辅基。通过沉降平衡法估计该酶的相对分子质量为74400。该酶是一种单体。已测定了氧化型和还原型纤维二糖氧化酶的光学、荧光和电子顺磁共振（e.p.r.）光谱。对纤维二糖氧化酶底物特异性的初步研究表明，二糖甚至一些不溶性多糖是底物，但单糖不是。在高浓度纤维二糖时可见强烈的底物抑制作用。当氧气作为电子受体时，这种效应尤为明显。纤维二糖氧化酶在黄素蛋白中是不寻常的，因为它能稳定红色阴离子黄素半醌并形成亚硫酸盐加合物，但似乎产生超氧阴离子作为其主要的还原氧产物。
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