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...
Main Authors: | Mathew, Sam, Deepankumar, Kanagavel, Shin, Giyoung, Hong, Eun Young, Kim, Byung-Gee, Chung, Taeowan, Yun, Hyungdon |
---|---|
Other Authors: | School of Materials Science & Engineering |
Format: | Journal Article |
Language: | English |
Published: |
2017
|
Subjects: | |
Online Access: | https://hdl.handle.net/10356/83502 http://hdl.handle.net/10220/42634 |
Similar Items
-
Microscale methods to rapidly evaluate bioprocess options for increasing bioconversion yields: application to the ω-transaminase synthesis of chiral amines
by: Halim, Murni, et al.
Published: (2014) -
Enzymatic synthesis of dilaurylazelate ester for nanocosmeceutical application
by: Khairudin, Nurshafira
Published: (2018) -
Effects of Phenolic Monomers on Enzymatic and Fermentation Activities of the Rumen Fungus, Neocallimastix Frontalis
by: Saad, Wan Zuhainis
Published: (2006) -
Kinetic study of asymmetric synthesis of chiral amine with immobilized transaminase
by: S. D., Vijaya Kumar, et al.
Published: (2019) -
Enzymatic Production Of Feruloylated Acylglycerols From Olive Fatty Acid Distillates As Sunscreen Agents
by: Kong, Ching
Published: (2008)