By a News Reporter-Staff News Editor at Life Science Weekly -- Current study results on Life Science Research have been published. According to news reporting from Taipei, Taiwan, by NewsRx journalists, research stated, "In this study, we synthesized water-soluble hyperbranched poly(amido acid)s (HBPAAs) featuring multiple terminal CO2H units and internal tertiary amino and amido moieties and then used them in conjunction with an in situ Fe2+/Fe3+ co-precipitation process to prepare organic/magnetic nanocarriers comprising uniformly small magnetic iron oxide nanoparticles (NP) incorporated within the globular HBPAAs. Transmission electron microscopy revealed that the HBPAA-gamma-Fe2O3 NPs had dimensions of 6-11 nm, significantly smaller than those of the pristine gamma-Fe2O3 (20-30 nm)."
The news correspondents obtained a quote from the research from the Institute of Molecular Biology, "Subsequently, we covalently immobilized a bacterial.-glutamyltranspeptidase (BlGGT) upon the HBPAA-gamma-Fe2O3 nanocarriers through the formation of amide linkages in the presence of a coupling agent. Magnetization curves of the HBPAA-gamma-Fe2O3/BlGGT composites measured at 300 K suggested superparamagnetic characteristics, with a saturation magnetization of 52 emu g(-1). The loading capacity of BlGGT on the HBPAA-gamma-Fe2O3 nanocarriers was 16 mg g(-1) support; this sample provided a 48% recovery of the initial activity. The immobilized enzyme could be recycled 10 times with 32% retention of the initial activity; it had stability comparable with that of the free enzyme during a storage period of 63 days."
According to the news reporters, the research concluded: "The covalent immobilization and stability of the enzyme and the magnetization provided by the HBPAA-gamma-Fe2O3 NPs suggests that this approach could be an economical means of depositing bioactive enzymes upon nanocarriers for BlGGT-mediated bio-catalysis."
For more information on this research see: Surface-Functionalized Hyperbranched Poly(Amido Acid) Magnetic Nanocarriers for Covalent Immobilization of a Bacterial gamma-Glutamyltranspeptidase. Molecules, 2014;19(4):4997-5012. Molecules can be contacted at: Mdpi Ag, Postfach, Ch-4005 Basel, Switzerland. (Springer - www.springer.com; Molecules - www.springerlink.com/content/1420-3049/)
Our news journalists report that additional information may be obtained by contacting T.Y. Juang, Academy Sinica, Inst Mol Biol, Taipei 11529, Taiwan. Additional authors for this research include S.J. Kan, Y.Y. Chen, Y.L. Tsai, M.G. Lin and L.L. Lin (see also Life Science Research).
Keywords for this news article include: Asia, Taipei, Taiwan, Life Science Research
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