Purification of Mutarotase, Extracted from Bovine Kidney Cortex

Bovine kidney cortex was homogenized to extract mutarotase that was subjected to ammonium sulfate precipitation, ion exchange and gel filtration chromatographic techniques. The activity and specific activity of crude enzyme was observed as 1.27 and 0.34 U mg-1, respectively which was increased by 3.52 and 2.55 U mg-1 after partial purification by ammonium sulfate precipitation and desalting. The enzyme was then subjected to DEAE column for ion exchange chromatography and the resultant activity and specific activity gained by the enzyme was 3.17 and 2.50 U mg-1, respectively. After gel filtration chromatography through sephadex G-150, the observed activity and specific activity was 2.894 and 3.36 U mg-1 which indicates 9.97 fold purification.