Title of article :
Production and properties of threonine aldolase immobilisates
Author/Authors :
Kurjatschij، نويسنده , , Sandra and Katzberg، نويسنده , , Michael and Bertau، نويسنده , , Martin، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2014
Pages :
7
From page :
3
To page :
9
Abstract :
Dichiral β-hydroxy-α-amino acids are a highly valuable class of compounds from which pharmaceutically active intermediates for the synthesis of e.g. β-sympathomimetic drugs can be obtained. In lieu of laborious multi-step “classical” organic synthesis, biocatalysis using threonine aldolases (TAs) opens up a way to synthesise β-hydroxy-α-amino acids in one step. Although enzyme kinetics, stereospecificity as well as substrate specificity were and are matters of investigation, there is a lack of investigations addressing enzyme stability, which is crucial if the reaction is thought to be transferred to an economical scale. methods to immobilise the l-low specificity threonine aldolase of Escherichia coli (l-TA) were studied. After extensive screening the entrapment of the enzyme into a porous network of orthosilicate appeared to be the most promising method.
Keywords :
Enzyme immobilisation , Biocatalysis , amino alcohols , Threonine aldolase
Journal title :
Journal of Molecular Catalysis B Enzymatic
Serial Year :
2014
Journal title :
Journal of Molecular Catalysis B Enzymatic
Record number :
1718688
Link To Document :
بازگشت