Tanzania
Research Article
Characterization of a High Activity (S)-Aminotransferase for Substituted (S)-Aminotetralin Production: Properties and Kinetics
Author(s): Abraham R. Martin, David Shonnard, Sachin Pannuri and Sanjay KamatAbraham R. Martin, David Shonnard, Sachin Pannuri and Sanjay Kamat
The production of substituted (S)-Aminotetralins requires biocatalyst that have high activities at high temperatures and considerable tolerance to amine donors to shift the reaction towards products. The biocatalyst used in this process are (S)-Aminotransferases. An (S)-aminotransferase of a high activity derived from Athrobacter citreous by directed evolution for the production of substituted (S)-aminotetralin was characterized in the form of whole cells. Its optimum conditions were pH 7 and 55 °C. Maximum activity was 0.21 mM/min per gram of whole cells. Substrate affinities were 750 mM for isopropylamine and 10.4 mM for substituted tetralone. A kinetic study to describe the production of substituted (S)-aminotetralin showed that two major reactions were involved: one enzyme catalyzed –by (S)-aminotransferase- that is the production of subs.. Read More»
DOI:
10.4172/2155-9821.1000107
Journal of Bioprocessing & Biotechniques received 3351 citations as per Google Scholar report