Identification of novel thermostable omega-transaminase and its application for enzymatic synthesis of chiral amines at high temperature

A novel thermostable omega-transaminase from Thermomicrobium roseum which showed broad substrate specificity and high enantio-selectivity 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.