Abstract
The initial action patterns of saccharifying α- and liquefying α-amylase of Bacillus subtilis on various β-limit dextrins were investigated and the following results were obtained:
1) The initial attack of saccharifying α-amylase occurred much more readily at the third or more inner bond toward the reducing end from the branching point.
2) In the case of liquefying α-amylase, the amylase seemed to hydrolyze the glucosidic linkage at the fifth or more inner bond from the branching point.
These observations were quite comparable with the results obtained by using linear maltooligosaccharides in the earlier report*, where the glucosidic linkages to be split by these amylases are determined by the certain distance from the non-reducing end of the saccharides.
