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Item type:Publication, Access status: without files , New functional amorphous calcium phosphate nanocomposites by enzyme-assisted biomineralization(American Chemical Society (ACS), 2013-12-31); ; ; In the present study, we report on enzyme-assisted formation of biomineralized amorphous calcium phosphate nanocomposites (ACP-NCs). About 100-200 nm sizes of the spherical porous enzyme-assisted ACP-NCs were successfully synthesized via double reverse microemulsion, but no ACP-NCs formed without the enzyme. It is believed that the enzyme was used as an organic template or additive that could regulate the biomineralization process. The enzyme-assisted ACP-NCs were well characterized by X-ray diffraction, transmission electron microscopy, scanning electron microscopy, dynamic light scattering, and Brunauer-Emmett-Teller (BET) criteria. The BET surface area, total pore volume, pore size from adsorption, and pore size from desorption of the ACP-NCs were 163 m2 g-1 or 0.37 cm3 g -1, 8.87 nm, and 7.48 nm, respectively. The enzyme-assisted ACP-NCs retained about 43% of the catalytic activity of free carboxyl esterase. Furthermore, they preserved their bioactivity even after the 10th reuse and were stable over 10 days even under a stringent shaking conditions. The reported method paves the way for novel biomineralization via enzyme molecules to form functional enzymes containing nanocomposites.Publicationtype: Journal Article98 - Some of the metrics are blocked by yourconsent settings
Item type:Publication, Access status: without files , Magnetic-separable robust microbeads using a branched polymer for stable enzyme immobilizationUniform magnetic separable robust microbeads using a branched polymer were successfully developed for stable enzyme immobilization. The changed morphology of the microbeads was shown by scanning electron microscopy (SEM) analysis. The aldehyde groups on the polymers and imine groups derived from the Schiff base reaction between the aldehyde and amine moiety were found as the evidence of these reactions based on Fourier transform infrared (FT-IR) spectroscopy. The amine groups of the enzyme react with the aldehyde groups on the glutaraldehyde polymer so that the stable conjugations are formed. The specific activity of the conjugated enzyme was found to be retained more than 50%, but the reaction rate constant, Km value was not changed, compared to the free enzyme. In addition, the enzyme conjugated in the microbeads was found to be highly stable for more than 50 days, pertaining over 60% of its initial activity, even after being reused more than 15 times repeatedly. Furthermore, the magnetic-driven controllability provided facile separable characters for the repeated recycling. It is expected that these microbeads can be utilized as a key tool for successful realization not only in enzymatic conversion processes but also in extended fields; bio-based sensors or analytical devices, bioprocessing, bioremediation, to name only a few of numerous areas.Publicationtype: Journal Article30