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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
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