Abstract
The hydrolyzing activity of taka-diastase to carboxymethylderivatives of polysaccharides is still uncertain, therefore the action of taka-diastase to both carboxymethylstarch (CMS) and carboxymethylcellulose (CMC) was investigated. The degree of hydrolysis of the substrate was determined by measuring the formation of the total reducing sugars, according to the procedure of Somogyi. Taka-diastase hydrolyzed CMS and CMC to nearly same levels, though it was less effective than in the case of starch. Between CMS and CMC no significant differences were found in regard to the optimal pH or temperature and the rate of hydrolysis in the presence of some enzyme inhibitors. Even heating of the enzyme did not produce any differences of hydrolysis between both substrates. Taka-amylase A (TAA) and taka-amylase B (TAB) were prepared from taka-diastase, according to the method of Akabori et al. and Okazaki. The former could hydrolyze more strongly CMS than CMC for the first several hours in incubating, while the latter showed always a considerable hydrolyzing activity to CMC but not to CMS. The paper chromatogram of the incubation mixture of CMC and TAB mainly indicated the formation of glucose along with a few oligosaccharides. However, such activity of TAB might be due to a contamination of a hydrolyzing enzyme such as cellulase, because its activity for CMC progressively decreased with its further purification.
