Identification and characterization of proteinase B as an unstable factor for neutral lactase in the enzyme preparation from Kluyveromyces lactis.

The stability of the commercial lactase enzyme is important for the dairy industry. A destabilizing factor for neutral lactase in the enzyme preparation from Kluyveromyces lactis was investigated. We found that lactase had lower thermal stability when fragmented bands of lactase were confirmed on SDS-PAGE.

Characterization of two amine oxidases from Aspergillus carbonarius AIU 205.

We have reported that Aspergillus carbonarius AIU 205, which was isolated by our group, produced three enzymes exhibiting oxidase activity for 4-aminobutanamide (4-ABAD) (J. Biosci. Bioeng.

New enzymatic methods for selective assay of L-lysine using an L-lysine specific decarboxylase/oxidase from Burkholderia sp. AIU 395.

We developed new enzymatic methods for the selective assay of L-lysine by utilizing an oxidase reaction and a decarboxylation reaction by the L-lysine-specific decarboxylase/oxidase (L-Lys-DC/OD) from Burkholderia sp. AIU 395. The method utilizing the oxidase reaction of this enzyme was useful for determination of high concentrations of L-lysine.

Characterization of a pyridoxal-5'-phosphate-dependent l-lysine decarboxylase/oxidase from Burkholderia sp. AIU 395.

A novel enzyme, which catalyzed decarboxylation of l-lysine into cadaverine with release of carbon dioxide and oxidative deamination of l-lysine into l-2-aminoadipic 5-semialdehyde with release of ammonia and hydrogen peroxide, was found from a newly isolated Burkholderia sp. AIU 395. The enzyme was specific to l-lysine and did not exhibit enzyme activities for other l-amino acids, l-lysine derivatives, d-amino acids, and amines.

Mutational and crystallographic analysis of l-amino acid oxidase/monooxygenase from Pseudomonas sp. AIU 813: Interconversion between oxidase and monooxygenase activities.

In this study, it was shown for the first time that l-amino acid oxidase of Pseudomonas sp. AIU813, renamed as l-amino acid oxidase/monooxygenase (l-AAO/MOG), exhibits l-lysine 2-monooxygenase as well as oxidase activity. l-Lysine oxidase activity of l-AAO/MOG was increased in a p-chloromercuribenzoate (p-CMB) concentration-dependent manner to a final level that was five fold higher than that of the non-treated enzyme.

Characterization and application of aminoamide-oxidizing enzyme from Aspergillus carbonarius AIU 205.

We isolated Aspergillus carbonarius AIU 205 as a new producer of an enzyme catalyzing oxidative deamination of 4-aminobutanamide (4-ABAD) to 4-oxobutanamide with the subsequent release of ammonia and hydrogen peroxide. Since the strain produced three enzymes with different Km values for 4-ABAD, the enzyme with lowest Km value (0.31 mM) was purified and revealed certain remarkable properties.

Purification and characterization of an L-amino acid oxidase from Pseudomonas sp. AIU 813.

An L-amino acid oxidase was found from a newly isolated strain, Pseudomonas sp. AIU 813. This enzyme was remarkably induced by incubation with L-lysine as a nitrogen source, and efficiently purified using an affinity chromatography with L-lysine as ligand.

Microscopic evidence for the stacking faults and metallic properties of a triangular lattice CoO(2) with a three-layer structure.

Stacking faults and metallic properties for the triangular lattice system CoO(2), which has basically three oxygen layers with a prismatic oxygen environment between the layers, have been explored mainly through measurements of nuclear magnetic and quadrupole resonance. A significant distribution of the quadrupole frequency for (59)Co nuclei, due to stacking faults and short atomic coherence, is found. The spin dynamics is successfully understood in terms of the relaxation mechanism for a weakly correlated metal system.