Abstract
1. The actions of p-phenylazobenzoyl Taka-amylase A (PhAB-TAA) on phenyl α-maltotrioside and on malto-oligosaccharides were compared with those of intact Taka-amylase A (TAA).
2. On conversion of TAA to PhAB-TAA by introduction of a p-phenylazobenzoyl residue the action changed as follows: with phenyl α-maltotrioside as substrate PhAB-TAA produced more phenol and less phenyl α-glucoside than TAA. However, with maltopentaitol as substrate, the actions of PhAB-TAA and TAA were similar.
3. It was concluded that the p-phenylazobenzoyl residue was introduced into the enzyme molecule very close to the catalytic site and its interaction with the phenyl residue in the substrate created the difference between the actions of intact and modified TAA.
