Table 1 α-Chymotrypsin activity values.

From: Perchlorate salts confer psychrophilic characteristics in α-chymotrypsin

 

kcat (s−1)

KM (μM)

kcat/KM (M−1 s−1)

308 K

278 K

308 K

278 K

308 K

278 K

Buffer

71.23

12.66

72.60

24.66

9.81 × 105

5.13 × 105

+ Glycine

74.99

14.17

67.41

12.80

1.11 × 106

1.11 × 106

1 M NaClO4

67.47

15.02

91.49

27.49

7.37 × 105

5.46 × 105

+ Glycine

61.07

14.93

77.48

18.43

7.88 × 105

8.10 × 105

0.25 M Mg(ClO4)2

61.76

15.47

121.30

34.37

5.09 × 105

4.50 × 105

+ Glycine

62.55

17.73

73.40

19.35

8.52 × 105

9.16 × 105

0.5 M Mg(ClO4)2

36.58

10.54

54.05

4.72

6.77 × 105

2.23 × 106

+ Glycine

42.43

15.65

83.04

25.67

5.11 × 105

6.10 × 105

  1. The turnover number (kcat), Michaelis constant (KM) and catalytic efficiency (kcat/KM) of α-chymotrypsin at 308 K (35 °C) and 278 K (5 °C) in the presence and absence of perchlorate salts and 1 M glycine. Kinetic parameters were determined from the Michaelis–Menten curves of n = 4 replicates.
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