Immobilization of Lipase onto Functional Cyclomatrix Polyphosphazene Microspheres

Publication date: Available online 5 July 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Chen Chen, Xue-yan Zhu, Qiao-ling Gao, Fei Fang, Li-wei Wang, Xiao-Jun Huang Functional polyphosphazene cyclomatrix microspheres (PMS) containing glucose and dodecyl moieties were utilized for physical adsorption of lipase. In this regard, Candia Rugosa lipase was immobilized onto the above microspheres through physical adsorption, which exhibited catalytic hydrolysis of glycerol triacetate as the model reaction. As observed under transmission electron microscope (TEM) and scanning electron microscope (SEM), the size of all the microspheres ranged from 400nm to 1μm with a mean diameter of 680nm. Zeta potential analysis demonstrated that the microspheres were negatively charged. The influences of buffer pH, substrate concentration and temperature were also studied along with reusability. The obtained results demonstrated that the immobilized lipase on deprotected glycosylated PMS (D-GPMS) showed the best performance and possessed the highest enzymatic loading activity around 1.0884mmol.L−1 min−1 g−1, and retained nearly 50% of its initial activity even after 10 cycles of application. Moreover, the lipase-microsphere complex displayed high pH adaptability from 7 to 9 and temperature stability above 40°C. From the viewpoint of biocompatible PMS support, the GPMS-lipase conjugate have potential applications in field such as food, medicine and enviro...
Source: Journal of Molecular Catalysis B: Enzymatic - Category: Biochemistry Source Type: research