Purification and characterization of an intracellular peroxidase from Streptomyces cyaneus

Journal Article · Sun Mar 01 04:00:00 EST 1992 · Applied and Environmental Microbiology; (United States)

OSTI ID:7066652

Mliki, A; Zimmermann, W ^[1]

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1. ETH-Zuerich (Switzerland)

Peroxidases play an important role in the oxidation of a large number of aromatic compounds, including recalcitrant substances. An intracellular peroxidase (EC 1.11.1.7) from Streptomyces cyaneus was purified to homogeneity. The enzyme had a molecular weight of 185,000 and was composed of two subunits of equal size. It had an isoelectric point of 6.1. The enzyme had a peroxidase activity toward o-dianisidine with a K{sub m} of 17.8 {mu}M and a pH optimum of 5.0. It also showed catalase activity with a K{sub m} of 2.07 mM H{sub 2}O{sub 2} and a pH optimum of 8.0. The purified enzyme did not catalyze C{alpha}-C{beta} bond cleavage of 1,3-dihydroxy-2-(2-methoxyphenoxy)-1-(4-ethoxy-3-methoxyphenyl) propane, a nonphenolic dimeric lignin model compound. The spectrum of te peroxidase showed a soret band at 405 nm, which disappeared after reduction with sodium dithionite, indicating that the enzyme is a hemoprotein. Testing the effects of various inhibitors on the enzyme activity showed that it is a bifunctional enzyme having catalase and peroxidase activities.

• OSTI ID: 7066652
• Journal Information: Applied and Environmental Microbiology; (United States), Journal Name: Applied and Environmental Microbiology; (United States) Vol. 58:3; ISSN 0099-2240; ISSN AEMID
• Country of Publication: United States
• Language: English

Related Subjects

550200* -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
AROMATICS
BACTERIA
BIOCHEMISTRY
BIODEGRADATION
CARBOHYDRATES
CATALASE
CHEMICAL COMPOSITION
CHEMICAL REACTIONS
CHEMISTRY
DECOMPOSITION
ENZYME ACTIVITY
ENZYME INHIBITORS
ENZYMES
FRACTIONATION
LIGNIN
MICROORGANISMS
ORGANIC COMPOUNDS
OXIDOREDUCTASES
PEROXIDASES
POLYSACCHARIDES
PROTEINS
PURIFICATION
SACCHARIDES
SEPARATION PROCESSES
STREPTOMYCES