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Table 1 Summary of the procedure of GDH from Geotrichum candidum

From: Purification and characterization of a novel glutamate dehydrogenase from Geotrichum candidum with higher alcohol and amino acid activity

Purification steps Volume (mL) Total protein (mg) Total activitya (U) Specific activityb (U mg/protein) Recoveryc (%) Purification foldd
Crude extract 100.0 85.11 8388.89 98.57 100.00 1
Ammonium sulfate (30–70%) 8.5 3.19 3630.43 1138.40 43.28 11.55
MonoQ anion-exchange chromatography 2.0 0.76 1838.61 2419.2 10 24.54
Sephacry S-200 5.4 0.06 239.57 3802.70 2.86 38.58
  1. All experiments were conducted at 4 °C. The 30 and 70% ammonium sulfate fractions were pooled and then subjected to MonoQ anion-exchange chromatography
  2. Significance of the difference (P ≤ 0.05). Mean ± SD from triplicate determinations
  3. aTotal activity = specific activity × total amount of protein
  4. bSpecific activity of GDH was tested using hexanol as a substrate
  5. cRecovery = (total protein of the fraction/total activity of crude extract) × 100%
  6. dPurification fold = specific activity of the fraction/specific activity of crude extract