Purification and properties of cellobiose: quinone oxidoreductase from Sporotrichum pulverulentum.
Purification and properties of cellobiose: quinone oxidoreductase from Sporotrichum pulverulentum.
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纤维二糖的纯化和性质：来自粉状孢子霉的醌氧化还原酶。
DOI：
10.3891/acta.chem.scand.29b-0419
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发表时间：
1975
期刊：
影响因子：
--
通讯作者：
K. Eriksson
中科院分区：
文献类型：
--
作者：
U. Westermark;K. Eriksson
通过硫酸铵沉淀、SP-Sephadex C-50 色谱法和羟基磷灰石柱色谱法纯化纤维二糖：醌氧化还原酶。通过超速离心和 SDS 凝胶电泳分析，纯化的酶是均质的。该酶是一种以 FAD 为辅基的黄素蛋白，产生纤维二糖氧化产物纤维二糖-δ-内酯。纤维五糖也被氧化，但未检测到纤维素的氧化。该酶氧化乳糖和 4-β-葡萄糖基甘露糖，但不氧化 4-β-甘露糖基葡萄糖，这表明二糖非还原端的 C-2-羟基对于底物特异性很重要。
Cellobiose: quinone oxidoreductase was purified by ammonium sulfate precipitation, SP-Sephadex C-50 chromatography, and hydroxylapatite column chromatography. The purified enzyme is homogeneous by ultracentrifugal and SDS-gel electrophoretic analyses. The enzyme is a flavoprotein with FAD as the prosthetic group and produces cellobiono-delta-lactone as the product of cellobiose oxidation. Cellopentaose is also oxidized but no oxidation of cellulose could be detected. The enzyme oxidizes lactose and 4-beta-glucosylmannose but not 4-beta-mannosylglucose which implicates the C-2-hydroxyl of the non-reducing end of the disaccharide as important for substrate specificity.