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Table 2 Substrate specificities of Sephadex G-200-purified hydrolytic enzymes

From: Characterization of β-galactosidase and α-galactosidase activities from the halophilic bacterium Gracilibacillus dipsosauri

Substrate

β-Galactosidase I

β-Galactosidase II

α-Galactosidase

β-ONP-Gal

100

100

5.6

α-ONP-Gal

2.7

3.1

164.6

β-PNP-Gal

41.6

183.8

3.5

α-PNP-Gal

0.7

2.7

100

β-PNP-Glc

1.

3.1

3.8

α-PNP-Glc

0.4

1.2

0.5

α-PNP-Ara

9.1

41.7

0.6

  1. Activities are expressed as a percentage of the activity with the primary substrate for each enzyme. The activities of the control reaction were 50 nmol min−1 ml−1 for β-galactosidase I with β-ONPG as the substrate, 43 nmol min−1 ml−1 for β-galactosidase II with β-ONPG as the substrate, and 127 nmol min−1 ml−1 for α-galactosidase with α-PNPG as the substrate