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Crosslinked enzyme aggregates in hierarchically-ordered mesoporous silica: A simple and effective method for enzyme stabilization

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dc.contributor.authorKim, Moon Il-
dc.contributor.authorKim, Jungbae-
dc.contributor.authorLee, Jinwoo-
dc.contributor.authorJia, Hongfei-
dc.contributor.authorBin Na, Hyon-
dc.contributor.authorYoun, Jong Kyu-
dc.contributor.authorKwak, Ja Hun-
dc.contributor.authorDohnalkova, Alice-
dc.contributor.authorGrate, Jay W.-
dc.contributor.authorWang, Ping-
dc.contributor.authorHyeon, Taeghwan-
dc.contributor.authorPark, Hyun Gyu-
dc.contributor.authorChang, Ho Nam-
dc.date.accessioned2020-04-27T13:28:26Z-
dc.date.available2020-04-27T13:28:26Z-
dc.date.issued2007-02-
dc.identifier.citationBiotechnology and Bioengineering, Vol.96 No.2, pp.210-218-
dc.identifier.issn0006-3592-
dc.identifier.other92831-
dc.identifier.urihttps://hdl.handle.net/10371/165896-
dc.description.abstractalpha-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.subjectCLEAs (crosslinked enzyme aggregates)-
dc.subjectalpha-chymotrypsin-
dc.subjectMucor javanicus lipase-
dc.subjectenzyme immobilization-
dc.subjectHMMS (hierarchically-ordered mesocellular mesoporous silica)-
dc.titleCrosslinked enzyme aggregates in hierarchically-ordered mesoporous silica: A simple and effective method for enzyme stabilization-
dc.typeArticle-
dc.contributor.AlternativeAuthor현택환-
dc.identifier.doi10.1002/bit.21107-
dc.citation.journaltitleBiotechnology and Bioengineering-
dc.identifier.scopusid2-s2.0-33846932034-
dc.citation.endpage218-
dc.citation.number2-
dc.citation.startpage210-
dc.citation.volume96-
dc.identifier.urlhttps://onlinelibrary.wiley.com/doi/abs/10.1002/bit.21107-
dc.identifier.rimsid92831-
dc.identifier.sci000243449100002-
dc.description.isOpenAccessN-
dc.contributor.affiliatedAuthorHyeon, Taeghwan-
Appears in Collections:
College of Engineering/Engineering Practice School (공과대학/대학원)Dept. of Chemical and Biological Engineering (화학생물공학부)Journal Papers (저널논문_화학생물공학부)
College of Engineering/Engineering Practice School (공과대학/대학원)Dept. of Chemical and Biological Engineering (화학생물공학부)Chemical Convergence for Energy and Environment (에너지환경 화학융합기술전공)Journal Papers (저널논문_에너지환경 화학융합기술전공)
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