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Lee, D.,Lee, J.,Kim, J.,Kim, J.,Na, H. B.,Kim, B.,Shin, C.-H.,Kwak, J. H.,Dohnalkova, A.,Grate, J. W.,Hyeon, T.,Kim, H.-S. WILEY-VCH Verlag 2005 Advanced Materials Vol.17 No.23
<B>Graphic Abstract</B> <P>Glucose oxidase immobilized in mesocellular carbon foam results in a highly sensitive and fast glucose biosensor. The structure of the mesocellular foam (see Figure), with a combination of mesopores containing the glucose oxidase (GOx) enzymes and micropores and transport channels, results in high enzyme loading and low mass-transfer limitations, producing higher catalytic activity and sensitivity than polymer-matrix-based GOx glucose sensors. <img src='wiley_img/09359648-2005-17-23-ADMA200500793-content.gif' alt='wiley_img/09359648-2005-17-23-ADMA200500793-content'> </P>
Lee, Jinwoo,Na, Hyon Bin,Kim, Byoung Chan,Lee, Jin Hyung,Lee, Byoungsoo,Kwak, Ja Hun,Hwang, Yosun,Park, Je-Geun,Gu, Man Bock,Kim, Jaeyun,Joo, Jin,Shin, Chae-Ho,Grate, Jay W.,Hyeon, Taeghwan,Kim, Jungb Royal Society of Chemistry 2009 Journal of materials chemistry Vol.19 No.42
<P>A magnetically-separable and highly-stable enzyme system was developed by adsorption of enzymes in superparamagnetic hierarchically ordered mesocellular mesoporous silica (M-HMMS) and subsequent enzyme crosslinking. Superparamagnetic nanoparticles were homogeneously incorporated into hierarchically-ordered mesocellular mesoporous silica (HMMS) by the decomposition of a preformed iron propionate complex. The size of the incorporated superparamagnetic nanoparticles was around 5 nm, generating a magnetically separable host with high pore volumes and large pores (M-HMMS). α-chymotrypsin (CT) was adsorbed into M-HMMS with high loading (∼30 wt%) in less than 30 minutes. Glutaraldehyde (GA) treatment of adsorbed CT resulted in nanometer scale crosslinked enzyme aggregates in M-HMMS (CLEA-M). The activity of these CT aggregates in M-HMMS (CLEA-M-CT) was 34 times than that of simply adsorbed CT in M-HMMS, due to an effective prevention of enzyme leaching during washing <I>via</I> a ship-in-a-bottle approach. CLEA-M-CT maintained the initial activity not only under shaking (250 rpm) for 30 days, but also under recycled uses of 35 times. The same approach was employed for the synthesis of CLEA-M of lipase (CLEA-M-LP), and proven to be effective in improving the loading, activity, and stability of enzyme when compared to those of adsorbed LP in M-HMMS.</P> <P>Graphic Abstract</P><P>Crosslinked enzyme aggregates in magnetitie-coated mesoporous silica, fabricated <I>via</I> a two-step procedure of enzyme adsorption and crosslinking, were highly active, highly stable, and easily recyclable using a magnet. <IMG SRC='http://pubs.rsc.org/services/images/RSCpubs.ePlatform.Service.FreeContent.ImageService.svc/ImageService/image/GA?id=b909109b'> </P>
Highly stable trypsin-aggregate coatings on polymer nanofibers for repeated protein digestion
Kim, Byoung Chan,Lopez-Ferrer, Daniel,Lee, Sang-Mok,Ahn, Hye-Kyung,Nair, Sujith,Kim, Seong H.,Kim, Beom Soo,Petritis, Konstantinos,Camp, David G.,Grate, Jay W.,Smith, Richard D.,Koo, Yoon-Mo,Gu, Man B WILEY-VCH Verlag 2009 Proteomics Vol.9 No.7
<P>A stable and robust trypsin-based biocatalytic system was developed and demonstrated for proteomic applications. The system utilizes polymer nanofibers coated with trypsin aggregates for immobilized protease digestions. After covalently attaching an initial layer of trypsin to the polymer nanofibers, highly concentrated trypsin molecules are crosslinked to the layered trypsin by way of a glutaraldehyde treatment. This process produced a 300-fold increase in trypsin activity compared with a conventional method for covalent trypsin immobilization, and proved to be robust in that it still maintained a high level of activity after a year of repeated recycling. This highly stable form of immobilized trypsin was resistant to autolysis, enabling repeated digestions of BSA over 40 days and successful peptide identification by LC-MS/MS. This active and stable form of immobilized trypsin was successfully employed in the digestion of yeast proteome extract with high reproducibility and within shorter time than conventional protein digestion using solution phase trypsin. Finally, the immobilized trypsin was resistant to proteolysis when exposed to other enzymes (i.e., chymotrypsin), which makes it suitable for use in “real-world” proteomic applications. Overall, the biocatalytic nanofibers with trypsin aggregate coatings proved to be an effective approach for repeated and automated protein digestion in proteomic analyses.</P>
Kim, Moon Il,Kim, Jungbae,Lee, Jinwoo,Jia, Hongfei,Na, Hyon Bin,Youn, Jong Kyu,Kwak, Ja Hun,Dohnalkova, Alice,Grate, Jay W.,Wang, Ping,Hyeon, Taeghwan,Park, Hyun Gyu,Chang, Ho Nam Wiley Subscription Services, Inc., A Wiley Company 2007 Biotechnology and bioengineering Vol.96 No.2
<P>α-chymotrypsin (CT) and lipase (LP) were immobilized in hierarchically-ordered mesocellular mesoporous silica (HMMS) in a simple but effective way for the enzyme stabilization, which was achieved by the enzyme adsorption followed by glutaraldehyde (GA) crosslinking. This resulted in the formation of nanometer scale crosslinked enzyme aggregates (CLEAs) entrapped in the mesocellular pores of HMMS (37 nm), which did not leach out of HMMS through narrow mesoporous channels (13 nm). CLEA of α-chymotrypsin (CLEA-CT) in HMMS showed a high enzyme loading capacity and significantly increased enzyme stability. No activity decrease of CLEA-CT was observed for 2 weeks under even rigorously shaking condition, while adsorbed CT in HMMS and free CT showed a rapid inactivation due to the enzyme leaching and presumably autolysis, respectively. With the CLEA-CT in HMMS, however, there was no tryptic digestion observed suggesting that the CLEA-CT is not susceptible to autolysis. Moreover, CLEA of lipase (CLEA-LP) in HMMS retained 30% specific activity of free lipase with greatly enhanced stability. This work demonstrates that HMMS can be efficiently employed as host materials for enzyme immobilization leading to highly enhanced stability of the immobilized enzymes with high enzyme loading and activity. Biotechnol. Bioeng. 2007;96: 210–218. © 2006 Wiley Periodicals, Inc.</P>