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DC Field | Value | Language |
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dc.citation.endPage | 214 | - |
dc.citation.startPage | 209 | - |
dc.citation.title | JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC | - |
dc.citation.volume | 97 | - |
dc.contributor.author | Kim, Min Hoo | - |
dc.contributor.author | Park, Saerom | - |
dc.contributor.author | Kim, Yong Hwan | - |
dc.contributor.author | Won, Keehoon | - |
dc.contributor.author | Lee, Sang Hyun | - |
dc.date.accessioned | 2023-12-22T03:10:27Z | - |
dc.date.available | 2023-12-22T03:10:27Z | - |
dc.date.created | 2016-09-06 | - |
dc.date.issued | 2013-12 | - |
dc.description.abstract | We employed a cross-linked enzyme aggregate (CLEA) method to immobilize formate dehydrogenase (FDH) from Candida boidinii. The optimal conditions for the preparation of CLEAs were determined by examining effects of various parameters: the nature and amount of cross-linking reagent, additive concentration, cross-linking time, and pH during CLEA preparation. The recovered activities of CLEAs were significantly dependent on the concentration of glutaraldehyde; however, the recovered activity was not severely influenced by the content of dextran polyaldehyde as a mild cross-linker. Bovine serum albumin (BSA) was also used as a proteic feeder and enhanced the activity recovery by 130%. The highest recovered activity of CLEA was 18% for formate oxidation reaction and 25% for CO2 reduction reaction. The residual activity of CLEA prepared with dextran polyaldehyde (Dex-CLEA) was over 95% after 10 cycles of reuse. The thermal stability of Dex-CLEA was increased by a factor of 3.6 more than that of the free enzyme. CLEAs of FDH could be utilized efficiently for both NADH regeneration and CO2 reduction. | - |
dc.identifier.bibliographicCitation | JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC, v.97, pp.209 - 214 | - |
dc.identifier.doi | 10.1016/j.molcatb.2013.08.020 | - |
dc.identifier.issn | 1381-1177 | - |
dc.identifier.scopusid | 2-s2.0-84884312606 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/20349 | - |
dc.identifier.url | http://www.sciencedirect.com/science/article/pii/S138111771300249X | - |
dc.identifier.wosid | 000327005000031 | - |
dc.language | 영어 | - |
dc.publisher | ELSEVIER SCIENCE BV | - |
dc.title | Immobilization of formate dehydrogenase from Candida boidinii through cross-linked enzyme aggregates | - |
dc.type | Article | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
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