Isolation and Characterization of Immobilized Aminoacylase from Streptoverticillium olivoreticuli

Immobilization of aminoacylase from Streptoverticillium olivoreticuli by incorporation into acrylamide gel has been investigated. The data showed that the process should be carried out at constant pH. Thermal inactivation of the immobilized enzyme under the reaction conditions was studied. The kinetics of enzymatic stereospecific deacylation of N-acetyl-DL-phenylalanine was analyzed. The results of this study may be used in the synthesis of amino acid enantiomers.