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báo cáo khoa học: "Examination of Cholesterol oxidase attachment to magnetic nanoparticles"

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Tuyển tập báo cáo các nghiên cứu khoa học quốc tế ngành y học dành cho các bạn tham khảo đề tài: Examination of Cholesterol oxidase attachment to magnetic nanoparticles | Journal of Nanobiotechnology BioMed Central Research Open Access Examination of Cholesterol oxidase attachment to magnetic nanoparticles Gilles K Kouassi1 Joseph Irudayaraj 1 and Gregory McCarty2 Address department of Agricultural and Biological Engineering 249 Agricultural Engineering Building The Pennsylvania State University University Park PA 16802 USA and department of Engineering Sciences and Mechanics The Pennsylvania State University University Park PA 16802 USA Email Gilles K Kouassi - gkk2@psu.edu Joseph Irudayaraj - josephi@psu.edu Gregory McCarty - GMcCrty@psu.edu Corresponding author Published 20 January 2005 Received 20 September 2004 Accepted 20 January 2005 Journal of Nanobiotechnology 2005 3 1 doi 10.1186 1477-3 155-3-1 This article is available from http www.jnanobiotechnology.com content 3 1 1 2005 Kouassi et al licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License http creativecommons.Org licenses by 2.0 which permits unrestricted use distribution and reproduction in any medium provided the original work is properly cited. Abstract Magnetic nanoparticles Fe3O4 were synthesized by thermal co-precipitation of ferric and ferrous chlorides. The sizes and structure of the particles were characterized using transmission electron microscopy TEM . The size of the particles was in the range between 9.7 and 56.4 nm. Cholesterol oxidase CHO was successfully bound to the particles via carbodiimide activation. FTIR spectroscopy was used to confirm the binding of CHO to the particles. The binding efficiency was between 98 and 100 irrespective of the amount of particles used. Kinetic studies of the free and bound CHO revealed that the stability and activity of the enzyme were significantly improved upon binding to the nanoparticles. Furthermore the bound enzyme exhibited a better tolerance to pH temperature and substrate concentration. The activation energy for free and bound CHO was

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