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Xanthomonas axonopodis pv로 부터 새로운 SGNH family member의 동정
| DC Field | Value | Language |
|---|---|---|
| dc.contributor.advisor | 김 두 헌 | - |
| dc.contributor.author | 김남용 | - |
| dc.date.accessioned | 2018-11-08T08:17:42Z | - |
| dc.date.available | 2018-11-08T08:17:42Z | - |
| dc.date.issued | 2014-02 | - |
| dc.identifier.other | 16095 | - |
| dc.identifier.uri | https://dspace.ajou.ac.kr/handle/2018.oak/12483 | - |
| dc.description | 학위논문(석사)--아주대학교 일반대학원 :분자과학기술학과,2014. 2 | - |
| dc.description.tableofcontents | Abstract ⅰ List of Figures ⅱ Ⅰ. Introduction 1 1.1. Backgrounds 1 Ⅱ. Materials and methods 3 2.1. Materials 3 2.2. Cloning, expression, and purification of 833 3 2.3. Primary sequence analysis and homology modeling 4 2.4. Substrate specificity 5 2.5. pH stability of 833 5 2.6. Thermostability of 833 5 2.7. Chemical stability of 833 6 Ⅲ. Results and Discussion 7 3.1. Analysis of the sequence of 833 7 3.2. Purification of 833 using affinity binding chromatography 9 3.3. Molecular modeling of 833 10 3.4. Functional analysis of 833 11 Ⅳ. Conclusions 19 Ⅴ. Appendix 20 Reference 20 | - |
| dc.language.iso | eng | - |
| dc.publisher | The Graduate School, Ajou University | - |
| dc.rights | 아주대학교 논문은 저작권에 의해 보호받습니다. | - |
| dc.title | Xanthomonas axonopodis pv로 부터 새로운 SGNH family member의 동정 | - |
| dc.title.alternative | Kim Nam Yong | - |
| dc.type | Thesis | - |
| dc.contributor.affiliation | 아주대학교 일반대학원 | - |
| dc.contributor.alternativeName | Kim Nam Yong | - |
| dc.contributor.department | 일반대학원 분자과학기술학과 | - |
| dc.date.awarded | 2014. 2 | - |
| dc.description.degree | Master | - |
| dc.identifier.localId | 608161 | - |
| dc.identifier.url | http://dcoll.ajou.ac.kr:9080/dcollection/jsp/common/DcLoOrgPer.jsp?sItemId=000000016095 | - |
| dc.subject.keyword | SGNH hydrolase | - |
| dc.description.alternativeAbstract | A novel putative lysophospholipase hydrolase (833) from Xanthomonas axonopodis pv was identified, characterized. Sequence analysis of 833 revealed a putative catalytic triad (Ser61, Asp209, and His212), and a conserved sequence motif Ser(S)61-Gly(G)126-Asn(N)128-His(H)212 with moderate identities with other members of the SGNH-hydrolase superfamily. 833 was able to hydrolyze short-chain esters such as p-nitrophenyl acetate (C2), butyrate (C4), and valerate (C5) suggesting that the hydrophobic binding pocket of 833 seems to be optimized to accommodate short acyl chain lengths. 833 displayed its maximal activity at pH 7.0 , 60 °C. Higher thermal and chemical stability of the 833 highlight its potential applicability as a biocatalyst in the pharmaceutical and chemical industries. | - |
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- Graduate School of Ajou University > Department of Molecular Science and Technology > 3. Theses(Master)
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