DC Field | Value | Language |
---|---|---|
dc.contributor.author | Shin, Woo-Ri | ko |
dc.contributor.author | Um, Hyun-Ju | ko |
dc.contributor.author | Kim, Young-Chang | ko |
dc.contributor.author | Kim, Sun Chang | ko |
dc.contributor.author | Cho, Byung-Kwan | ko |
dc.contributor.author | Ahn, Ji-Young | ko |
dc.contributor.author | Min, Jiho | ko |
dc.contributor.author | Kim, Yang-Hoon | ko |
dc.date.accessioned | 2021-02-26T08:10:18Z | - |
dc.date.available | 2021-02-26T08:10:18Z | - |
dc.date.created | 2021-02-18 | - |
dc.date.issued | 2021-01 | - |
dc.identifier.citation | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, v.168, pp.403 - 411 | - |
dc.identifier.issn | 0141-8130 | - |
dc.identifier.uri | http://hdl.handle.net/10203/281062 | - |
dc.description.abstract | We identified three novel microbial esterase (Est1, Est2, and Est3) from Sphingobium chungbukense DJ77. Multiple sequence alignment showed the Est1 and Est3 have distinct motifs, such as tetrapeptide motif HGGG, a pentapeptide sequencemotif GXSXG, and catalytic triad residues Ser-Asp-His, indicating that the identified enzymes belong to family IV esterases. Interestingly, Est1 exhibited strong activity toward classical esterase substrates, pnitrophenyl ester of short-chain fatty acids and long-chain. However, Est3 did not exhibit any activity despite having high sequence similarity and sharing the identical catalytic active residues with Est1. Est3 only showed hydrolytic degradation activity to polycaprolactone (PCL). MOE-docking prediction also provided the parameters consisting of binding energy, molecular docking score, and molecular distance between substrate and catalytic nucleophilic residue, serine. The engineered mutEst3 has hydrolytic activity for a variety of esters ranging from p-nitrophenyl esters to PCL. In the present study, we demonstrated that MOE-docking simulation provides a valuable insight for facilitating biocatalytic performance. | - |
dc.language | English | - |
dc.publisher | ELSEVIER | - |
dc.title | Biochemical characterization and molecular docking analysis of novel esterases from Sphingobium chungbukense DJ77 | - |
dc.type | Article | - |
dc.identifier.wosid | 000608018200041 | - |
dc.identifier.scopusid | 2-s2.0-85097885535 | - |
dc.type.rims | ART | - |
dc.citation.volume | 168 | - |
dc.citation.beginningpage | 403 | - |
dc.citation.endingpage | 411 | - |
dc.citation.publicationname | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES | - |
dc.identifier.doi | 10.1016/j.ijbiomac.2020.12.077 | - |
dc.contributor.localauthor | Kim, Sun Chang | - |
dc.contributor.localauthor | Cho, Byung-Kwan | - |
dc.contributor.nonIdAuthor | Shin, Woo-Ri | - |
dc.contributor.nonIdAuthor | Um, Hyun-Ju | - |
dc.contributor.nonIdAuthor | Kim, Young-Chang | - |
dc.contributor.nonIdAuthor | Ahn, Ji-Young | - |
dc.contributor.nonIdAuthor | Min, Jiho | - |
dc.contributor.nonIdAuthor | Kim, Yang-Hoon | - |
dc.description.isOpenAccess | N | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordAuthor | Sphingobium chungbukense | - |
dc.subject.keywordAuthor | DJ77 | - |
dc.subject.keywordAuthor | Esterase | - |
dc.subject.keywordAuthor | Biochemical characterization | - |
dc.subject.keywordAuthor | Molecular docking analysis | - |
dc.subject.keywordPlus | ENZYMATIC-HYDROLYSIS | - |
dc.subject.keywordPlus | RATIONAL DESIGN | - |
dc.subject.keywordPlus | LIPASE | - |
dc.subject.keywordPlus | CLASSIFICATION | - |
dc.subject.keywordPlus | FAMILY | - |
dc.subject.keywordPlus | CATALYSIS | - |
dc.subject.keywordPlus | SEQUENCE | - |
dc.subject.keywordPlus | BINDING | - |
dc.subject.keywordPlus | SINGLE | - |
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