固定化在氨丙基玻璃上提高了 L-阿拉伯糖异构酶的活性和稳定性。
Enhanced activity and stability of L-arabinose isomerase by immobilization on aminopropyl glass.
机构信息
Department of Chemical Engineering, Konkuk University, Seoul 143-701, South Korea.
出版信息
Appl Microbiol Biotechnol. 2011 Mar;89(5):1435-42. doi: 10.1007/s00253-010-2966-8. Epub 2010 Oct 31.
Immobilization of Bacillus licheniformis L: -arabinose isomerase (BLAI) on aminopropyl glass modified with glutaraldehyde (4 mg protein g support⁻¹) was found to enhance the enzyme activity. The immobilization yield of BLAI was proportional to the quantity of amino groups on the surface of support. Reducing particle size increased the adsorption capacity (q(m)) and affinity (k(a)). The pH and temperature for immobilization were optimized to be pH 7.1 and 33 °C using response surface methodology (RSM). The immobilized enzyme was characterized and compared to the free enzyme. There is no change in optimal pH and temperature before and after immobilization. However, the immobilized BLAI enzyme achieved 145% of the activity of the free enzyme. Correspondingly, the catalytic efficiency (k(cat)/K(m)) was improved 1.47-fold after immobilization compared to the free enzyme. The thermal stability was improved 138-fold (t₁/₂) increased from 2 to 275 h) at 50 °C following immobilization.
固定化地衣芽孢杆菌 L: -阿拉伯糖异构酶（BLAI）于戊二醛改性的氨基丙基玻璃（4 mg 蛋白 g 载体⁻¹）上被发现可提高酶活性。BLAI 的固定化产率与载体表面氨基基团的数量成正比。减小粒径增加了吸附容量（q(m)）和亲和力（k(a)）。使用响应面法（RSM）优化了固定化的 pH 和温度，分别为 pH 7.1 和 33°C。对固定化酶进行了表征，并与游离酶进行了比较。固定化前后最佳 pH 和温度没有变化。然而，固定化的 BLAI 酶的活性达到了游离酶的 145%。相应地，与游离酶相比，固定化后的酶的催化效率（k(cat)/K(m)）提高了 1.47 倍。固定化后，酶的热稳定性提高了 138 倍（t₁/₂）从 2 小时增加到 275 小时）在 50°C 下。
Zotero 插件