Ghadi Arezoo, Tabandeh Fatemeh, Mahjoub Soleiman, Mohsenifar Afshin, Roshan Farid Talebnia, Alavije Razieh Shafiee
Department of Industrial and Environmental Biotechnology, National Institute of Genetic Engineering and Biotechnology (NIGEB) Tehran, ( 2) Faculty of Chemical Engineering, Noshirvani University of Technology, Babol, Iran.
J Oleo Sci. 2015;64(4):423-30. doi: 10.5650/jos.ess14236.
In this study, the chitosan magnetic core-shell nanoparticles (CMNPs) was synthesized and then used as a support for immobilization of lipase. The characteristics of CMNPs, including morphology, topography and spectra type before and after immobilization were determined. The scanning electron micrographs of the CMNPs showed that they were approximately uniform spheres and the distribution chart indicated that the particles have the mean diameter of 100 nm. Kinetic parameters of Km and Vm were calculated as 1.07 mM and 29.43 U/mg for free B. cepacia lipase and 1.29 mM and 25.82 U/mg for immobilized lipase on CMNPs, respectively. The activity of immobilized lipase was 32 U/mg under optimum temperature and pH. CMNP's were used in trasesterification reaction in order to evaluate the activity of the immobilized enzyme compared to the free enzyme. Immobilization of lipase on CMNPs improved stability and total relative activity of the enzyme. It could be concluded that CMNPs be considered as a suitable carrier for enzyme immobilization.
在本研究中,合成了壳聚糖磁性核壳纳米粒子(CMNPs),然后将其用作固定化脂肪酶的载体。测定了CMNPs固定化前后的形态、形貌和光谱类型等特性。CMNPs的扫描电子显微镜图像显示它们近似为均匀的球体,分布图表明颗粒的平均直径为100nm。游离洋葱伯克霍尔德菌脂肪酶的米氏常数(Km)和最大反应速率(Vm)动力学参数分别计算为1.07mM和29.43U/mg,而固定在CMNPs上的脂肪酶的Km和Vm分别为1.29mM和25.82U/mg。在最佳温度和pH条件下,固定化脂肪酶的活性为32U/mg。使用CMNPs进行转酯化反应,以评估固定化酶与游离酶相比的活性。脂肪酶固定在CMNPs上提高了酶的稳定性和总相对活性。可以得出结论,CMNPs可被视为酶固定化的合适载体。