Identification of novel thermostable ω-transaminase and its application for enzymatic synthesis of chiral amines at high temperature
A novel thermostable ω-transaminase from Thermomicrobium roseum which showed broad substrate specificity and high enantioselectivity was identified, expressed and biochemically characterized. The advantage of this enzyme to remove volatile inhibitory by-products was demonstrated by performing asymme...
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sg-ntu-dr.10356-835022020-06-01T10:13:44Z Identification of novel thermostable ω-transaminase and its application for enzymatic synthesis of chiral amines at high temperature Mathew, Sam Deepankumar, Kanagavel Shin, Giyoung Hong, Eun Young Kim, Byung-Gee Chung, Taeowan Yun, Hyungdon School of Materials Science & Engineering Omega-transaminases Enzymatic synthesis A novel thermostable ω-transaminase from Thermomicrobium roseum which showed broad substrate specificity and high enantioselectivity was identified, expressed and biochemically characterized. The advantage of this enzyme to remove volatile inhibitory by-products was demonstrated by performing asymmetric synthesis and kinetic resolution at high temperature. 2017-06-09T03:20:35Z 2019-12-06T15:24:22Z 2017-06-09T03:20:35Z 2019-12-06T15:24:22Z 2016 2016 Journal Article Mathew, S., Deepankumar, K., Shin, G., Hong, E. Y., Kim, B.-G., Chung, T., et al. (2016). Identification of novel thermostable ω-transaminase and its application for enzymatic synthesis of chiral amines at high temperature. RSC Advances, 6(73), 69257-69260. https://hdl.handle.net/10356/83502 http://hdl.handle.net/10220/42634 10.1039/C6RA15110H 199972 en RSC Advances © 2016 The Royal Society of Chemistry |
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Omega-transaminases Enzymatic synthesis |
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Omega-transaminases Enzymatic synthesis Mathew, Sam Deepankumar, Kanagavel Shin, Giyoung Hong, Eun Young Kim, Byung-Gee Chung, Taeowan Yun, Hyungdon Identification of novel thermostable ω-transaminase and its application for enzymatic synthesis of chiral amines at high temperature |
| description |
A novel thermostable ω-transaminase from Thermomicrobium roseum which showed broad substrate specificity and high enantioselectivity was identified, expressed and biochemically characterized. The advantage of this enzyme to remove volatile inhibitory by-products was demonstrated by performing asymmetric synthesis and kinetic resolution at high temperature. |
| author2 |
School of Materials Science & Engineering |
| author_facet |
School of Materials Science & Engineering Mathew, Sam Deepankumar, Kanagavel Shin, Giyoung Hong, Eun Young Kim, Byung-Gee Chung, Taeowan Yun, Hyungdon |
| format |
Article |
| author |
Mathew, Sam Deepankumar, Kanagavel Shin, Giyoung Hong, Eun Young Kim, Byung-Gee Chung, Taeowan Yun, Hyungdon |
| author_sort |
Mathew, Sam |
| title |
Identification of novel thermostable ω-transaminase and its application for enzymatic synthesis of chiral amines at high temperature |
| title_short |
Identification of novel thermostable ω-transaminase and its application for enzymatic synthesis of chiral amines at high temperature |
| title_full |
Identification of novel thermostable ω-transaminase and its application for enzymatic synthesis of chiral amines at high temperature |
| title_fullStr |
Identification of novel thermostable ω-transaminase and its application for enzymatic synthesis of chiral amines at high temperature |
| title_full_unstemmed |
Identification of novel thermostable ω-transaminase and its application for enzymatic synthesis of chiral amines at high temperature |
| title_sort |
identification of novel thermostable ω-transaminase and its application for enzymatic synthesis of chiral amines at high temperature |
| publishDate |
2017 |
| url |
https://hdl.handle.net/10356/83502 http://hdl.handle.net/10220/42634 |
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1681056424777482240 |