Abstract
The enzyme transaminase carry potential to be used for industrial applications directed towards production of chiral amines and amino acids. The present study was directed towards isolation, purification and immobilization of one such transaminase from Moraxella sp. NCIM 2795. Partial purification of enzyme was performed by ammonium sulphate precipitation technique. The partially purified enzyme was subjected to different immobilization techniques like physical adsorption, ionic binding, covalent binding using chitin and chitosan beads respectively. The effect of various immobilization and chemical modification parameters along with the effect of amine donors, storage stability and reusability on transaminase enzyme activity were evaluated. The transaminase enzyme assays for acetophenone conversion were performed by GC.
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