Cumhuriyet University, Department of Molecular Biology and Genetics, Sivas 58140, Turkey.
Int J Biol Macromol. 2012 May 1;50(4):991-5. doi: 10.1016/j.ijbiomac.2012.02.011. Epub 2012 Mar 3.
A Thermoalkalophilic amylase was produced from an environmental bacterial isolate. The enzyme was then immobilized through its amino groups onto the epoxy rings of magnetic poly glycidyl methacrylate [m-poly (GMA)] beads. The free enzyme was active within a large pH range, between 7 and 12 and displayed the optimum activity at 95°C and pH 10. The immobilization appeared to increase the stability of the enzyme as its bound form showed optimum activity at 105°C and pH 11.0. Kinetic studies demonstrated that immobilized enzyme had higher K(m) and lower V(max) values. The activity of the free and bound enzyme was determined, at 37°C and pH 10.0 and pH 11.0, respectively, in the presence of various organic solvents and detergents (5%, v/v). Results obtained indicated that detergents, sodium dodecyl sulfate (SDS) and TritonX-100, caused six fold increase and that various organic solvents also increased the activity of the amylase.
一种嗜热耐碱淀粉酶是从环境细菌分离株中产生的。然后，通过其氨基将酶固定在磁性聚甲基丙烯酸缩水甘油酯 [m-聚（GMA）] 珠上的环氧环上。游离酶在较大的 pH 范围内（7 至 12）具有活性，并在 95°C 和 pH 10 时显示出最佳活性。固定化似乎提高了酶的稳定性，因为其结合形式在 105°C 和 pH 11.0 时显示出最佳活性。动力学研究表明，固定化酶具有更高的 K(m)值和更低的 V(max)值。在 37°C 和 pH 10.0 和 pH 11.0 下，分别在存在各种有机溶剂和洗涤剂（5％，v/v）的情况下测定了游离酶和结合酶的活性。结果表明，洗涤剂十二烷基硫酸钠（SDS）和 TritonX-100 使酶的活性增加了六倍，并且各种有机溶剂也增加了淀粉酶的活性。
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