JPS5814198B

A novel peroxidase for reduced nicotinamide-adenine-dinucleotide is provided which peroxidase oxidizes reduced nicotinamide-adenine-dinucleotide with hydrogen peroxide to give nicotinamide-adenine-dinucleotide and water and is characterized by a Michaelis constant KM to hydrogen peroxide of 2.8x10-5...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Hauptverfasser:	KURAUSU BOOKANPU, DETOREFU FUON HERUSHERUMAN, HANSU ZAIDERU, HANSU MERERINKU, PEETAA SHUTAARU, ARUBERUTO REEDAA, BORUFUGANKU GURUUBAA
Format:	Patent
Sprache:	eng
Schlagworte:	BEER BIOCHEMISTRY CHEMISTRY COMPOSITIONS OR TEST PAPERS THEREFOR COMPOSITIONS THEREOF CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL ORENZYMOLOGICAL PROCESSES CULTURE MEDIA ENZYMOLOGY INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIRCHEMICAL OR PHYSICAL PROPERTIES MEASURING MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEICACIDS OR MICROORGANISMS METALLURGY MICROBIOLOGY MICROORGANISMS OR ENZYMES MUTATION OR GENETIC ENGINEERING PHYSICS PROCESSES OF PREPARING SUCH COMPOSITIONS PROPAGATING, PRESERVING OR MAINTAINING MICROORGANISMS SPIRITS TESTING VINEGAR WINE
Online-Zugang:	Volltext bestellen
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Beschreibung
Zusammenfassung:	A novel peroxidase for reduced nicotinamide-adenine-dinucleotide is provided which peroxidase oxidizes reduced nicotinamide-adenine-dinucleotide with hydrogen peroxide to give nicotinamide-adenine-dinucleotide and water and is characterized by a Michaelis constant KM to hydrogen peroxide of 2.8x10-5M and to reduced nicotinamide-adenine-dinucleotide of 1.7x10-5M, measured at 25 DEG C. in 0.2M tris buffer of pH 6.0, containing 0.1M potassium acetate. The peroxidase can be prepared by liberating the enzyme from Streptococcus faecalis ATCC 8043 by digestion or by treatment with a surface-active agent and isolating same from the enzyme solution obtained. Hydrogen peroxide is determined in a simple reaction or in a coupled reaction with a specific oxidase by contacting the said peroxidase with the H2O2 producing reaction mixture at a pH of from 6.0 to 9.0 and measuring the change of extinction as a measure of H2O2 and of the concentration of nicotinamide-adenine-dinucleotide initially present in said reaction mixture.