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Modular multi-enzyme cascade process using highly stabilized enzyme microbeads
Chung, Jinyang,Hwang, Ee Taek,Kim, Ji Hoon,Kim, Byoung Chan,Gu, Man Bock The Royal Society of Chemistry 2014 GREEN CHEMISTRY Vol.16 No.3
<P>A highly stable, homogeneous and magnetically separable enzyme microbead (EMB) comprised of branched-polymer/silica-shell hybrid microbeads is demonstrated. In addition, an EMB-based modular <I>in vitro</I> cascade reaction system is successfully implemented to the multi-enzymatic reactions with reusability and tractability.</P> <P>Graphic Abstract</P><P>A highly stable, homogeneous and magnetically separable enzyme microbead (EMB) comprised of branched-polymer/silica-shell hybrid microbeads is demonstrated. In addition, an EMB-based modular <I>in vitro</I> cascade reaction system is successfully implemented to the multi-enzymatic reactions with reusability and tractability. <IMG SRC='http://pubs.rsc.org/services/images/RSCpubs.ePlatform.Service.FreeContent.ImageService.svc/ImageService/image/GA?id=c3gc41737a'> </P>
Carbonic anhydrase assisted calcium carbonate crystalline composites as a biocatalyst
Hwang, Ee Taek,Gang, Haemin,Chung, Jinyang,Gu, Man Bock The Royal Society of Chemistry 2012 GREEN CHEMISTRY Vol.14 No.8
<P>In the present study, we report on the carbonic anhydrase (CA)-assisted formation of biomineralized calcium carbonate crystalline composites (CCCCs). Ellipsoidal CCCCs, such as calcite polymorphism, in a micro-size range catalyzed by CA were successfully synthesized with polyethylene glycol and magnetic nanoparticles in the constant CO<SUB>2</SUB> pressure controlled chamber, for the first time. CA-assisted CCCCs characterized by X-ray diffraction, transmission electron microscopy, scanning electron microscopy, and dynamic light scattering, showed their crystalline phase with mesoporous property according to Fourier transform infrared and Brunauer–Emmett–Teller area. These CCCCs retained about 43% of free CA esterase activity. Furthermore, the magnet-based separation was also successful for the reuse of the CCCCs. As a result, the CCCCs produced preserved their catalytic activity even after its ten repeated usages, and were stable for more than 50 days under room temperature. The reported method paves the way for novel biomineralization <I>via</I> CA for the formation of functional CA containing nanocomposites and biocatalyst technology applications.</P> <P>Graphic Abstract</P><P>Carbonic anhydrase-assisted calcium carbonate crystalline composites as a reusable biocatalyst. <IMG SRC='http://pubs.rsc.org/services/images/RSCpubs.ePlatform.Service.FreeContent.ImageService.svc/ImageService/image/GA?id=c2gc35444f'> </P>
New Functional Amorphous Calcium Phosphate Nanocomposites by Enzyme-Assisted Biomineralization
Hwang, Ee Taek,Tatavarty, Rameshwar,Chung, Jinyang,Gu, Man Bock American Chemical Society 2013 ACS APPLIED MATERIALS & INTERFACES Vol.5 No.3
<P>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 m<SUP>2</SUP> g<SUP>–1</SUP> or 0.37 cm<SUP>3</SUP> g<SUP>–1</SUP>, 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.</P><P><B>Graphic Abstract</B> <IMG SRC='http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/aamick/2013/aamick.2013.5.issue-3/am302580p/production/images/medium/am-2012-02580p_0010.gif'></P>