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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Main Authors: | , , , , , , |
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Other Authors: | |
Format: | Article |
Language: | English |
Published: |
2017
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Subjects: | |
Online Access: | https://hdl.handle.net/10356/83502 http://hdl.handle.net/10220/42634 |
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Institution: | Nanyang Technological University |
Language: | English |
Summary: | 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. |
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