TY - JOUR
T1 - Characterization of a High Activity (S)-Aminotransferase for Substituted (S)-Aminotetralin Production: Properties and Kinetics
AU - Mártin García, Abraham
AU - Shonnard, David R.
AU - Pannuri, Sachin
AU - Kamat, Sanjay Venkatesh
PY - 2011/11/17
Y1 - 2011/11/17
N2 - 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 substituted (S)-aminotetralin from isopropylamine and substituted tetralone; the other a non-enzyme catalyzed reaction that forms a byproduct consisting in the imine formed by substituted tetralone and substituted (S)-aminotetralin.
AB - 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 substituted (S)-aminotetralin from isopropylamine and substituted tetralone; the other a non-enzyme catalyzed reaction that forms a byproduct consisting in the imine formed by substituted tetralone and substituted (S)-aminotetralin.
UR - http://dx.doi.org/10.4172/2155-9821.1000107
U2 - 10.4172/2155-9821.1000107
DO - 10.4172/2155-9821.1000107
M3 - Artículo
JO - Journal of Bioprocessing & Biotechniques
JF - Journal of Bioprocessing & Biotechniques
SN - 2155-9821
ER -