Adsorption of Some β-Glycosidases on N-(g-Aminohexanoyl)-β-D-glycosylamine-agarose

抄録

Adsorption of β-galactosidase (EC 3. 2. 1. 23), β-glucosidase (EC 3. 2. 1. 21) and β-acetyl-glucosaminidase (EC 3. 2. 1. 30) on agarose substituted with N-(ε-aminohexanoyl)-β-D-galactosylamine, -β-D-glucosylamine, -2-acetamido-2-deoxy-β-D-glucosylamine and -β-D-mannosylamine was studied. All the glycosidases were adsorbed only at low buffer concentration. Although the adsorptions of Taka-diastase and Sanactase glycosidases were non-biospecific, the adsorption required the presence of the glycone as a ligand and the elution patterns in column chromatography were affected by variation of the glycone moiety of the adsorbent. The adsorptions of the enzymes on galactosylamine-agarose were prevented by low concentrations of hexoses and pentoses. The adsorption and desorption of emulsin glycosidase were apparently biospecific considering that the enzyme protein has one binding site for glucoside and one for galactoside, although the biospecificity was inexplicable in view of the large K₁ values of the spacerligand compounds.