Qing-Zhou Zhai* and Qing-Shuang Wang Pages 1 - 18 ( 18 )
Background: The development and applications of biological products were seriously hindered by the conventional immobilization of protein for its long-period, low efficiency, and high cost. The immobilization of protein on solid supports is an area of intense research due to the widespread use of immobilized protein in synthetic chemistry and industry. This paper describes a great interest in the adsorption of enzyme in the solid porous structured material and the design of new controlled delivery systems. The enzyme is immobilized in solid supports and synthetic materials of the reaction mixture with strong mechanical force and easy separation are served as a high selectivity catalyst.
Objective: A novel protein delivery system for the hemoglobin (Hb) enzyme was proposed by incorporating luminescence molecules into the mesopores of well-ordered hexagonal nanometer MCM (Mobil Composition of Matters) - 41. The prepared adsorbents were successfully applied to the design and synthesis of new functional luminescent materials. Various parameters affecting adsorption process such as adsorption time, the structures and loadings of MCM-41, the adsorption isotherm, and the reusability of adsorbent were investigated.
Method: The interaction between Hb and the MCM-41 was investigated using powder X-ray diffraction (XRD), Fourier infrared spectroscopy, UV-visible solid diffuse reflectance spectroscopy, luminescence spectroscopy, 77 K low temperature N2 adsorption-desorption study.
Results: The experimental parameters were optimized including the concentrations of the immobilized Hb, and the amounts of MCM-41 and the interior surface of phenyl-functionalized MCM-41 materials. Under the optimized conditions, the biocatalytic performance was studied for Hb/MCM-41 and Hb/Ph-(MCM-41).
Conclusion: The adsorption process of Hb by MCM-41 / Ph-(MCM-41) was in accord with the quasi-two-order kinetic model. The reuse activity experimental results indicating that the immobilized enzyme exhibited the high catalytic activity and thermal stability. Reusability stability and luminescence studies suggested that the prepared composites retained its activity even after 5 recycling runs and had some luminescence properties. The present results demonstrate that Hb/MCM41 and Hb/Ph-(MCM-41) are highly efficient potential nanobiocatalysts for the immobilization of enzymes onto mesoporous materials.
hemoglobin, immobilization, nanometer MCM-41, catalytic performance, composites, adsorption.
Research Center for Nanotechnology, South Campus, Changchun University of Science and Technology, 7186 Weixing Road, Changchun 130022, Jilin Province, Research Center for Nanotechnology, South Campus, Changchun University of Science and Technology, 7186 Weixing Road, Changchun 130022, Jilin Province