Abstract
Adenylate deaminase (AMPD, EC 3.5.4.6) is an aminohydrolase that widely used in the food and medicine industries. In this study, the gene encoding Aspergillus oryzae AMPD was cloned and expressed in Escherichia coli. Induction with 0.75mM isopropyl β-D-l-thiogalactopyranoside resulted in an enzyme activity of 1773.9U/mL. Recombinant AMPD was purified to electrophoretic homogeneity using nickel affinity chromatography, and its molecular weight was calculated as 78.6kDa. Purified AMPD exhibited maximal activity at 35°C, pH6.0 and 30mMK+, with apparent K m and V max values of 2.7×10-4M and 77.5μmol/mg/min under these conditions. HPLC revealed that recombinant AMPD could effectively catalyse the synthesis of inosine-5'-monophosphate (IMP) with minimal by-products, indicating high specificity and suggesting that it could prove useful for IMP production.
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