Immobilization of α‐amylase via adsorption on magnetic particles coated with polyaniline
Immobilization of α‐amylase via adsorption on magnetic particles coated with polyaniline
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DOI：
10.1002/star.201500161
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发表时间：
2016-05
期刊：
影响因子：
2.3
通讯作者：
Mirjana Radovanovic;B. Jugović;M. Gvozdenović;B. Jokić;B. Grgur;B. Bugarski;Z. Knežević-Jugović
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文献类型：
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作者：
Mirjana Radovanovic;B. Jugović;M. Gvozdenović;B. Jokić;B. Grgur;B. Bugarski;Z. Knežević-Jugović
研究了聚苯胺包覆磁性粒子吸附固定α-淀粉酶的方法。通过场发射扫描电子显微镜（FESEM）对载体进行了表征。所获得的磁性颗粒是尺寸小于100 nm的纳米颗粒的团聚体。考察了固定化时间、初始酶浓度、pH值和温度等因素对固定化效果的影响。固定化的最佳pH、温度和时间分别确定为7、45°C和75 min。在5 mg/mL酶浓度下测定10/100 mg载体的最大吸附α-淀粉酶量。结果表明，α-淀粉酶通过吸附在聚苯胺包覆的磁性颗粒上，在pH值和温度方面具有稳定性。平衡数据与Langmuir等温模型的良好一致性证实了酶分子在磁性颗粒表面的单层覆盖，并发现在25°C下的最大吸附容量为55.6/100 mg载体。该生物催化剂在间歇反应器中在60°C下在淀粉水解中重复使用9个循环后保留其初始活性的55.5 ± 1.63%。固定化酶也显示出非常好的储存稳定性。
The immobilization of α‐amylase via adsorption on magnetic particles coated with polyaniline was studied. The support was characterized by field emission scanning electron microscopy (FESEM). The obtained magnetic particles were agglomerates of nanoparticles with sizes below 100 nm. The effects of various factors on immobilization, including time, the initial enzyme concentration, pH, and temperature, were examined. The optimum pH, temperature, and time for immobilization were established to be 7, 45°C and 75 min, respectively. The maximum amount of adsorbed α‐amylase of 10/100 mg support was determined at the 5 mg/mL enzyme concentration. It appeared that α‐amylase was stabilized in terms of pH and temperature by adsorption on magnetic particles coated with polyaniline. The good agreement of the equilibrium data with the Langmuir isotherm model confirmed the monolayer coverage of enzyme molecules on the surface of magnetic particles, and the maximum adsorption capacity was found to be 55.6/100 mg support at 25°C. The biocatalyst retained 55.5 ± 1.63% of its initial activity after nine cycles of reuse in starch hydrolysis at 60°C in a batch reactor. The immobilized enzyme also showed very good storage stability.