Biochemical Processing and Biomaterial Research Laboratory, Gazi University, 06500 Ankara, Turkey; Department of Chemistry, Faculty of Sciences, Gazi University, 06500 Ankara, Turkey.
Department of Chemistry, Faculty of Sciences, Gazi University, 06500 Ankara, Turkey.
Food Chem. 2017 Apr 15;221:1442-1450. doi: 10.1016/j.foodchem.2016.11.007. Epub 2016 Nov 2.
In this study, magnetic nanoparticles (FeO) were modified sequentially with silica (FeO@SiO), glycidyl methacrylate (GMA) by surface initiated atom transfer radical polymerization (SI-ATRP) and hexamethylene diamine (as a spacer arm). The p(GMA) grafted and SA modified form (i.e., FeO@SiO@pGMA-SA-3) was used for covalent immobilization of invertase (EC 3.2.1.26). The amount of immobilized enzyme on FeO@SiO@p(GMA) and FeO@SiO@p(GMA)-SA-3 was 36.1±0.9 and 33.4±1.3mg/g, respectively. The K and V values of immobilized invertase were found to be 39.4mmol/L and 349.5mmol/L min, and not significantly changed compared with free form (34.3mmol/L and 387.2mmol/Lmin), respectively, revealed that the applied protocol did not have any detrimental effect on the retained activity of immobilized invertase.
在这项研究中，磁性纳米粒子（FeO）依次用硅（FeO@SiO）、甲基丙烯酸缩水甘油酯（GMA）通过表面引发原子转移自由基聚合（SI-ATRP）和己二胺（作为间隔臂）进行修饰。接枝 p(GMA)和 SA 修饰形式（即 FeO@SiO@pGMA-SA-3）用于共价固定化蔗糖酶（EC 3.2.1.26）。固定在 FeO@SiO@p(GMA)和 FeO@SiO@p(GMA)-SA-3 上的酶量分别为 36.1±0.9 和 33.4±1.3mg/g。固定化蔗糖酶的 K 和 V 值分别为 39.4mmol/L 和 349.5mmol/L min，与游离形式（34.3mmol/L 和 387.2mmol/L min）相比没有明显变化，表明所采用的方案对固定化蔗糖酶的保留活性没有任何不利影响。
