Table IV.
Substrate specificity of rRsBGAL1 toward polysaccharides
| Substratea | Relative Activityb | Limit of Hydrolysisc |
|---|---|---|
| β-(1→3)-Galactan | 8 | 29 |
| β-(1→3)(1→6)-Galactan from P. zopfii | 2 | 3 |
| β-(1→4)-Galactan from lupin | 0.8 | 1 |
| Native AGP from radish roots | 3 | 3 |
| α-l-Arafase-treated AGP from radish roots | 4 | 16 |
| Native AGP from radish leaves | 4 | 1 |
| α-l-Arafase-treated AGP from radish leaves | 8 | 25 |
| PNP-β-Gal | 100 | –d |
a
The enzyme was incubated with polymers at a concentration of 5 mg mL−1 and 2 mm was employed for PNP-β-Gal.
b
Activity is expressed as percent of that (64.9 units mg protein−1) of PNP-β-Gal.
c
The reaction was carried out under the standard conditions, except for the concentration of the substrate (1 mg mL−1) and the amount (20 mU) of the enzyme for 16 h, followed by further incubation with the addition of an equal amount of the enzyme for another 10 h. The limit of hydrolysis was determined after the liberation of reducing sugars reached a plateau, and expressed as Gal equivalent against the total sugars in each substrate.
d
Not determined.