从白蚁（Anacanthotermes）中分离到的共生芽孢杆菌 CF96 产生的一种新型β-1,4 葡聚糖酶。
A novel beta-1,4 glucanase produced by symbiotic Bacillus sp. CF96 isolated from termite (Anacanthotermes).
机构信息
Department of Chemistry, Faculty of Science, Ferdowsi University of Mashhad, Mashhad, Iran.
Department of Chemistry, Faculty of Science, Ferdowsi University of Mashhad, Mashhad, Iran.
出版信息
Int J Biol Macromol. 2019 Jun 15;131:752-759. doi: 10.1016/j.ijbiomac.2019.03.124. Epub 2019 Mar 20.
A novel beta-1,4-glucanase was purified and characterized from symbiotic Bacillus sp. CF96 of termite. The SDS-PAGE and zymogram analyses revealed a molecular mass of 35.6 kDa. Optimal activity was at 50 °C and pH 5.5, while the enzyme was active over a wide range of temperature 20-80 °C and pH 4-10 and interestingly more than 60% of the maximum activity remained up to pH 9. The enzyme activity increased in the presence of hexane, chloroform and methanol (20% v/v). while, the enzyme activity was inhibited by metal ions such as Mn, Hg, Cu, Zn, Mg, Fe. The isolated enzyme was able to degrade carboxymethyl cellulose (CMC), avicel and cellulose. Cellobiose was the hydrolytic product of enzymatic reaction based on thin layer chromatography (TLC) analysis. Regarding beta-1,4 endo/exoglucanase activity and high temperature, pH and solvent stability, the enzyme has potential for various industrial applications especially in designing pesticide for termite.
一种新型的β-1,4-葡聚糖酶从白蚁共生芽孢杆菌 CF96 中被分离并鉴定。SDS-PAGE 和酶谱分析显示其分子量为 35.6 kDa。最适活性温度为 50°C，最适 pH 值为 5.5，然而该酶在 20-80°C 和 pH 值 4-10 的广泛温度和 pH 值范围内均具有活性，有趣的是，其在 pH 值 9 时仍保持超过 60%的最大活性。该酶在正己烷、氯仿和甲醇（20% v/v）存在下活性增加，而金属离子如 Mn、Hg、Cu、Zn、Mg、Fe 会抑制酶的活性。分离出的酶能够降解羧甲基纤维素（CMC）、微晶纤维素和纤维素。根据薄层层析（TLC）分析，纤维二糖是酶促反应的水解产物。鉴于其β-1,4 内切/外切葡聚糖酶活性、耐高温、耐酸碱和耐溶剂的特性，该酶在各种工业应用中具有潜力，特别是在设计用于白蚁的农药方面。
Zotero 插件