DC Field | Value | Language |
---|---|---|
dc.contributor.author | Kim, Moon Il | ko |
dc.contributor.author | Kim, Jungbae | ko |
dc.contributor.author | Lee, Jinwoo | ko |
dc.contributor.author | Jia, Hongfei | ko |
dc.contributor.author | Bin Na, Hyon | ko |
dc.contributor.author | Youn, Jong Kyu | ko |
dc.contributor.author | Kwak, Ja Hun | ko |
dc.contributor.author | Dohnalkova, Alice | ko |
dc.contributor.author | Grate, Jay W. | ko |
dc.contributor.author | Wang, Ping | ko |
dc.contributor.author | Hyeon, Taeghwan | ko |
dc.contributor.author | Park, Hyun Gyu | ko |
dc.contributor.author | Chang, Ho Nam | ko |
dc.date.accessioned | 2010-11-30T08:37:37Z | - |
dc.date.available | 2010-11-30T08:37:37Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 2007-02 | - |
dc.identifier.citation | BIOTECHNOLOGY AND BIOENGINEERING, v.96, no.2, pp.210 - 218 | - |
dc.identifier.issn | 0006-3592 | - |
dc.identifier.uri | http://hdl.handle.net/10203/20548 | - |
dc.description.abstract | alpha-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) cross-linking. 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 alpha-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. | - |
dc.description.sponsorship | This work was supported by grant No. (R01-2004-000-10293-0) from the Basic Research Program of the Korea Science & Engineering Foundation, and partly by the Brain Korea 21 project of the Ministry of Education. Jungbae Kim thanks U.S. Department of Energy (DOE) LDRD funds administrated by the Pacific Northwest National Laboratory, DARPA/MTO (Contract DE-AC05-76RL01830), and the DOE Office of Biological and Environmental Research under the Environmental Management Science Program. The research was performed in part at the W.R. Wiley Environmental Molecular Sciences Laboratory, a national scientific user facility sponsored by the U.S. Department of Energy’s Office of Biological and Environmental Research and located at Pacific Northwest National Laboratory. | en |
dc.language | English | - |
dc.language.iso | en_US | en |
dc.publisher | JOHN WILEY & SONS INC | - |
dc.subject | CATALYTIC ACTIVITY | - |
dc.subject | IMMOBILIZATION | - |
dc.subject | PROTEINS | - |
dc.subject | ACYLASE | - |
dc.subject | ENCAPSULATION | - |
dc.subject | BIOCATALYSIS | - |
dc.subject | CHYMOTRYPSIN | - |
dc.subject | CRYSTALS | - |
dc.subject | SUPPORT | - |
dc.subject | FOAMS | - |
dc.title | Crosslinked enzyme aggregates in hierarchically-ordered mesoporous silica: A simple and effective method for enzyme stabilization | - |
dc.type | Article | - |
dc.identifier.wosid | 000243449100002 | - |
dc.identifier.scopusid | 2-s2.0-33846932034 | - |
dc.type.rims | ART | - |
dc.citation.volume | 96 | - |
dc.citation.issue | 2 | - |
dc.citation.beginningpage | 210 | - |
dc.citation.endingpage | 218 | - |
dc.citation.publicationname | BIOTECHNOLOGY AND BIOENGINEERING | - |
dc.identifier.doi | 10.1002/bit.21107 | - |
dc.embargo.liftdate | 9999-12-31 | - |
dc.embargo.terms | 9999-12-31 | - |
dc.contributor.localauthor | Lee, Jinwoo | - |
dc.contributor.localauthor | Park, Hyun Gyu | - |
dc.contributor.localauthor | Chang, Ho Nam | - |
dc.contributor.nonIdAuthor | Kim, Jungbae | - |
dc.contributor.nonIdAuthor | Jia, Hongfei | - |
dc.contributor.nonIdAuthor | Bin Na, Hyon | - |
dc.contributor.nonIdAuthor | Youn, Jong Kyu | - |
dc.contributor.nonIdAuthor | Kwak, Ja Hun | - |
dc.contributor.nonIdAuthor | Dohnalkova, Alice | - |
dc.contributor.nonIdAuthor | Grate, Jay W. | - |
dc.contributor.nonIdAuthor | Wang, Ping | - |
dc.contributor.nonIdAuthor | Hyeon, Taeghwan | - |
dc.description.isOpenAccess | N | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordAuthor | CLEAs (crosslinked enzyme aggregates) | - |
dc.subject.keywordAuthor | alpha-chymotrypsin | - |
dc.subject.keywordAuthor | Mucor javanicus lipase | - |
dc.subject.keywordAuthor | enzyme immobilization | - |
dc.subject.keywordAuthor | HMMS (hierarchically-ordered mesocellular mesoporous silica) | - |
dc.subject.keywordPlus | CATALYTIC ACTIVITY | - |
dc.subject.keywordPlus | IMMOBILIZATION | - |
dc.subject.keywordPlus | PROTEINS | - |
dc.subject.keywordPlus | ACYLASE | - |
dc.subject.keywordPlus | ENCAPSULATION | - |
dc.subject.keywordPlus | BIOCATALYSIS | - |
dc.subject.keywordPlus | CHYMOTRYPSIN | - |
dc.subject.keywordPlus | CRYSTALS | - |
dc.subject.keywordPlus | SUPPORT | - |
dc.subject.keywordPlus | FOAMS | - |
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