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Biomedical subjects

Y Nitta

Publications and source records attributed to Y Nitta.

At least 163 records · Page 9Linked to original sources

Hydrolysis of phenyl beta-maltoside catalyzed by saccharifying alpha-amylase from Bacillus subtilis.

1. The hydrolytic reaction of phenyl beta-maltoside catalyzed by saccharifying alpha-amylase [EC 3.2.1.1] of Bacillus subtilis was studied at 25 degrees C and pH 5.4, by measuring the total reducing power and the amount of phenol liberated, and by thin layer chromatography. 2. The enzyme hydrolyzed phenyl beta-maltoside at the glucosidic linkage between the two glucose residues to form D-glucose and phenyl beta-D-glucoside. Besides these products, maltose, maltotriose, and phenyl beta-maltotrioside were also observed as reaction products. The identification of phenyl beta-maltotrioside is described in detail. The formation of these products was attributed to the transglycosylation reaction of the enzyme. The time course of reaction as followed by reducing power measurement showed an induction period of several minutes.

Amylases↗

L-amino acid dehydrogenases in Bacillus subtilis spores.

The presence of two kinds of l-amino acid dehydrogenase in resting spores of Bacillus subtilis was indicated. One of them was l-alanine dehydrogenase, which used only l-alanine as a substrate, and the other was nonspecific dehydrogenase, which used l-valine, l-isoleucine, l-leucine, and l-alanine (slightly) as substrates. Several properties of these dehydrogenases were compared.

Alanine↗