DC Field | Value | Language |
---|---|---|
dc.contributor.author | Young-Hoon Cheon | ko |
dc.contributor.author | Geun-Joong Kim | ko |
dc.contributor.author | Kim, Hak-Sung | ko |
dc.date.accessioned | 2009-12-07T03:10:44Z | - |
dc.date.available | 2009-12-07T03:10:44Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 2000 | - |
dc.identifier.citation | JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC, v.11, no.1, pp.29 - 35 | - |
dc.identifier.issn | 1381-1177 | - |
dc.identifier.uri | http://hdl.handle.net/10203/14275 | - |
dc.description.abstract | It was observed that tetrameric D-hydantoinase from Bacillus stearothermophilus SD1 is dissociated into monomers under operational conditions, resulting in a detrimental loss of its catalytic activity. As an approach to reduce the dissociation of subunits and to maintain its catalytic activity, intersubunit cross-linking was attempted by using EDC (1-ethyl-3-(3-dimethylaminopropyl) carbodiimide, hydrochloride). The cross-linking conditions were optimized in terms of stabilization and catalytic activity of the recovered enzyme. Cross-linked D-hydantoinase showed a four-fold longer half-life under operational conditions and was very stable even at an elevated temperature, whereas the native enzyme was almost completely deactivated. In addition, intersubunit cross-linking of D-hydantoinase also led to stabilization of the enzyme in the presence of 20% methanol and under acidic conditions. The cross-linked enzyme was more efficient in the conversion of substrate, which seems to be due to the increased stability of enzyme. (C) 2000 Elsevier Science B.V. All rights reserved. | - |
dc.language | English | - |
dc.language.iso | en_US | en |
dc.publisher | ELSEVIER SCIENCE BV | - |
dc.subject | THERMOSTABLE D-HYDANTOINASE | - |
dc.subject | BACILLUS-STEAROTHERMOPHILUS SD-1 | - |
dc.subject | ENZYME | - |
dc.subject | CROSSLINKING | - |
dc.subject | INACTIVATION | - |
dc.subject | EXPRESSION | - |
dc.subject | STABILITY | - |
dc.subject | PROTEINS | - |
dc.title | Stabilization of D-hydantoinase by intersubunit cross-linking | - |
dc.type | Article | - |
dc.identifier.wosid | 000089979200004 | - |
dc.identifier.scopusid | 2-s2.0-0034736423 | - |
dc.type.rims | ART | - |
dc.citation.volume | 11 | - |
dc.citation.issue | 1 | - |
dc.citation.beginningpage | 29 | - |
dc.citation.endingpage | 35 | - |
dc.citation.publicationname | JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC | - |
dc.identifier.doi | 10.1016/S1381-1177(00)00193-4 | - |
dc.embargo.liftdate | 9999-12-31 | - |
dc.embargo.terms | 9999-12-31 | - |
dc.contributor.localauthor | Kim, Hak-Sung | - |
dc.contributor.nonIdAuthor | Young-Hoon Cheon | - |
dc.contributor.nonIdAuthor | Geun-Joong Kim | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordAuthor | D-hydantoinase | - |
dc.subject.keywordAuthor | Bacillus stearothermophilus | - |
dc.subject.keywordAuthor | intersubunit cross-linking | - |
dc.subject.keywordAuthor | EDC (1-ethyl-3-(3-dimethylaminopropyl) carbodiimide,hydrochloride) | - |
dc.subject.keywordPlus | THERMOSTABLE D-HYDANTOINASE | - |
dc.subject.keywordPlus | BACILLUS-STEAROTHERMOPHILUS SD-1 | - |
dc.subject.keywordPlus | ENZYME | - |
dc.subject.keywordPlus | CROSSLINKING | - |
dc.subject.keywordPlus | INACTIVATION | - |
dc.subject.keywordPlus | EXPRESSION | - |
dc.subject.keywordPlus | STABILITY | - |
dc.subject.keywordPlus | PROTEINS | - |
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.