Identification, characterization, and immobilization of a novel YbfF esterase from Halomonas elongata
DC Field | Value | Language |
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dc.contributor.author | Yoo, Wanki | - |
dc.contributor.author | Kim, Booyoung | - |
dc.contributor.author | Jeon, Sangeun | - |
dc.contributor.author | Kim, Kyeong Kyu | - |
dc.contributor.author | Kim, T. Doohun | - |
dc.date.available | 2021-02-22T04:57:18Z | - |
dc.date.issued | 2020-12 | - |
dc.identifier.issn | 0141-8130 | - |
dc.identifier.issn | 1879-0003 | - |
dc.identifier.uri | https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/1000 | - |
dc.description.abstract | The YbfF esterase family, which has a bifurcated binding pocket for diverse ligands, could serve as excellent biocatalysts in industrial and biotechnological applications. Here, the identification, characterization, and immobilization of a novel YbfF esterase (YbfFHalomonas elongata) from Halomonas elongata DSM 2581 is reported. Biochemical characterization of YbfF was carried out using activity staining, chromatographic analysis, kinetic analysis, activity assay, acetic acid release, and pH-indicator-based hydrolysis. YbfFH.elongata displayed broad substrate specificity, including that for p-nitrophenyl esters, glucose pentaacetate, tert-butyl acetate, and β-lactam-containing compounds, with high efficiency. Based on a homology model of YbfFH.elongata, Trp237 in the substrate-binding pocket, a critical residue for catalytic activity and substrate specificity was identified and characterized. Furthermore, crosslinked enzyme aggregates and nanoflower formation were explored to enhance the chemical stability and recyclability of YbfFH.elongata. The present study is the first report of a YbfF esterase from extremophiles, and explains its protein stability, catalytic activity, substrate specificities and diversities, kinetics, functional residues, amyloid formation, and immobilization. © 2020 Elsevier B.V. | - |
dc.format.extent | 10 | - |
dc.language | 영어 | - |
dc.language.iso | ENG | - |
dc.publisher | Elsevier B.V. | - |
dc.title | Identification, characterization, and immobilization of a novel YbfF esterase from Halomonas elongata | - |
dc.type | Article | - |
dc.publisher.location | 네델란드 | - |
dc.identifier.doi | 10.1016/j.ijbiomac.2020.09.247 | - |
dc.identifier.scopusid | 2-s2.0-85092144931 | - |
dc.identifier.wosid | 000600768200104 | - |
dc.identifier.bibliographicCitation | International Journal of Biological Macromolecules, v.165, pp 1139 - 1148 | - |
dc.citation.title | International Journal of Biological Macromolecules | - |
dc.citation.volume | 165 | - |
dc.citation.startPage | 1139 | - |
dc.citation.endPage | 1148 | - |
dc.type.docType | Article | - |
dc.description.isOpenAccess | N | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.subject.keywordPlus | 4 nitrophenyl ester | - |
dc.subject.keywordPlus | acetic acid | - |
dc.subject.keywordPlus | acetic acid derivative | - |
dc.subject.keywordPlus | ester derivative | - |
dc.subject.keywordPlus | esterase | - |
dc.subject.keywordPlus | glucose pentaacetate | - |
dc.subject.keywordPlus | tert butylacetate | - |
dc.subject.keywordPlus | unclassified drug | - |
dc.subject.keywordPlus | YbfF esterase | - |
dc.subject.keywordPlus | Article | - |
dc.subject.keywordPlus | biochemical analysis | - |
dc.subject.keywordPlus | catalysis | - |
dc.subject.keywordPlus | chromatography | - |
dc.subject.keywordPlus | controlled study | - |
dc.subject.keywordPlus | enzyme analysis | - |
dc.subject.keywordPlus | enzyme assay | - |
dc.subject.keywordPlus | enzyme immobilization | - |
dc.subject.keywordPlus | enzyme kinetics | - |
dc.subject.keywordPlus | enzyme specificity | - |
dc.subject.keywordPlus | Halomonas | - |
dc.subject.keywordPlus | Halomonas elongata | - |
dc.subject.keywordPlus | hydrolysis | - |
dc.subject.keywordPlus | molecular model | - |
dc.subject.keywordPlus | molecular stability | - |
dc.subject.keywordPlus | nonhuman | - |
dc.subject.keywordPlus | pH measurement | - |
dc.subject.keywordPlus | protein cross linking | - |
dc.subject.keywordPlus | protein stability | - |
dc.subject.keywordPlus | sequence analysis | - |
dc.subject.keywordPlus | structure analysis | - |
dc.subject.keywordAuthor | Halomonas elongata | - |
dc.subject.keywordAuthor | Immobilization | - |
dc.subject.keywordAuthor | Substrate specificity | - |
dc.subject.keywordAuthor | YbfFHalomonas elongata | - |
dc.identifier.url | http://www.sciencedirect.com/science/article/pii/S0141813020346109 | - |
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