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Action of crystalline acid carboxypeptidase from Penicillium janthinellum.
On the Inducers of α-Amylase Formation in Aspergillus oryzae
It is reported that isomaltose and panose are the most effective inducers among a large number of sugars examined here, and the importance of transglucosidase action demonstrated in view of α-amylase formation is suggested.
LOCALIZATION OF CELL-BOUND α-AMYLASE IN ASPERGILLUS ORYZAE DEMONSTRATED BY FLUORESCENT-ANTIBODY TECHNIQUE
The activity of a-amylase in Aspergillus oryzae is generally found in the mycelium as well as in the culture medium, and it is suggested that a-anmvlase might be located on the cell surfaces.
Studies on the Reduction of Indigo in Industrial Fermentation Vat (VIII) On the Starch-hydrolyzing Activity of Strain No. S-8
Binding of α-amylase to the cell wall of Aspergillus oryzae
Phenopicolinic acid, a new microbial product inhibiting dopamine beta-hydroxylase.
Defluorination of Monofluoroacetate by Bacteria
Monofluoroacetate (FA) is well known as a toxic substance and has been used as an insecticide: C-F linkage of which is very stable. Bacteria, capable of being grown in a defined salt medium…
NAD-linked d-Glucose-isomerizing and d-Mannose-isomerizing Enzyme from Paracolobacterum aerogenoides
In the course of study on the D-glucose isomerase, a new type of iso merizing enzyme was found and was present in Bacillus megaterium A-1.
NAD-linkedd-Glucose-isomerizing andd-Mannose-isomerizing Enzyme fromParacolobacterum aerogenoides
Submerged production, purification, and crystallization of acid carboxypeptidase from Penicillium janthinellum IFO-8070.
Penicillium janthinellum IFO-8070 produced an acid carboxypeptidase of molecular weight 51,000 in a liquid medium at 25 C which was purified 330-fold from koji culture to yield a crystalline protein which was demonstrated by disc electrophoresis to be homogeneous.