Federal Research Center "Fundamentals of Fundamental Biotechnology", Russian Academy of Sciences, Moscow, 119071, Russia.
Department of Chemical Enzymology, Faculty of Chemistry, Lomonosov Moscow State University, Moscow, 119991, Russia.
Biochemistry (Mosc). 2021 Apr;86(4):489-495. doi: 10.1134/S000629792104009X.
Heterologous endo-xanthanase (EX) from the thermophilic planktomycete Thermogutta terrifontis strain was obtained using Penicillium verruculosum 537 (ΔniaD) expression system with the cellobiohydrolase 1 gene promoter. Homogeneous EX with a molecular weight of 23.7 kDa (pI 6.5) was isolated using liquid chromatography methods. This xanthan degrading enzyme also possesses the enzymatic activity towards CM-cellulose, β-glucan, curdlan, lichenan, laminarin, galactomannan, xyloglucan but not towards p-nitrophenyl derivatives of β-D-glucose, mannose and cellobiose. The temperature and pH optima of EX were 55°C and 4.0, respectively; the enzyme exhibited 90% of its maximum activity in the temperature range 50-60°C and pH 3-5.
从嗜热浮游生物Thermogutta terrifontis 菌株中获得了异源内切-黄原胶酶（EX），该酶使用产黄青霉 537（ΔniaD）表达系统，利用纤维二糖水解酶 1 基因启动子进行表达。通过液相色谱法分离出分子量为 23.7 kDa（pI 6.5）的均一 EX。这种黄原胶降解酶还具有对 CM-纤维素、β-葡聚糖、卡拉胶、昆布多糖、海藻糖、半乳甘露聚糖、木葡聚糖的酶活性，但对β-D-葡萄糖、甘露糖和纤维二糖的对硝基苯基衍生物没有活性。EX 的最适温度和 pH 值分别为 55°C 和 4.0；该酶在 50-60°C 的温度范围内和 pH 值 3-5 时表现出 90%的最大活性。
