Purification and characterization of extracellular 3.BETA.-hydroxysteroid oxidase produced by Streptoverticillium cholesterolicum.

Inouye, Yoshio; Taguchi, Kimiko; Fujii, Akemi; Ishimaru, Kaori; Nakamura, Shoshiro; Nomi, Ryosaku

doi:10.1248/cpb.30.951

Cited by 57 publications

(32 citation statements)

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“…This is used for the measurement of total serum cholesterol coupled with cholesterol esterase and peroxidase. 1) Cholesterol oxidases are produced by Brevibacterium,2) Rhodococcus, 3) Streptomyces, 4,5) Schyzophyllum,6) and Streptoverticillium 7) species. Brevibacterium sterolicum A TCC 21387 produces cholesterol oxidase in the culture filtrate.…”

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confidence: 99%

Hyperexpression and Analysis ofchoBEncoding Cholesterol Oxidase ofBrevibacterium sterolicuminEscherichia coliandStreptomyces lividans.

Ohta

Fujishiro

Yamaguchi

et al. 1992

Bioscience, Biotechnology, and Biochemistry

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confidence: 99%

Hyperexpression and Analysis ofchoBEncoding Cholesterol Oxidase ofBrevibacterium sterolicuminEscherichia coliandStreptomyces lividans.

Ohta

Fujishiro

Yamaguchi

et al. 1992

Bioscience, Biotechnology, and Biochemistry

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“…Streptomyces species produce cholesterol oxidase extracellularly (13,22). The enzyme is commonly used for the enzymatic transformation of cholesterol (2,29) and for determinations of cholesterol levels in clinical specimens by coupling with peroxidase (1).…”

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confidence: 99%

“…Cells of Streptomyces lividans carrying plasmid pCO-1 overproduce extracellular cholesterol oxidase when cultured in an appropriate medium. Cholesterol oxidases from Streptomyces species (14) and from other microorganisms, such as Schizophyllum commune (10,16), Streptoverticillium cholesterolicum (13), and Brevibacterium sterolicum (31), contain a covalently bound flavin component as a prosthetic group.…”

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confidence: 99%

Nucleotide sequence of the gene for cholesterol oxidase from a Streptomyces sp

et al. 1989

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The nucleotide sequence of a 2.1-kilobase-pair fragment containing the Streptomyces choA gene, which codes a secreted cholesterol oxidase, was determined. A single open reading frame encodes a mature cholesterol oxidase of 504 amino acids, with a calculated Mr of 54,913. The leader peptides extend over 42 amino acids and have the characteristics of a signal sequence, including basic amino acids near the amino terminus and a hydrophobic core near the signal cleavage site. Analyses of the total amino acid composition and amino acid sequencing of the first 21 amino acids from the N terminus of the purified extracellular enzyme agree with the values deduced from nucleotide sequencing data.

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“…Enzyme assay -the activity of the extracellular and membrane-bound enzymes was determined according to the method described in Inouye et al (13). To 0.4 ml of 125 mM Tris-HCl buffer, pH 7.5, was added 0.1 ml of enzyme solution, and the mixture was incubated in water bath at 37°C.…”

Section: Methodsmentioning

confidence: 99%

Some enzymatic properties of cholesterol oxidase produced by Brevibacterium sp

et al. 1999

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In this study we determined some properties of the cholesterol oxidase from a Brevibacterium strain isolated from buffalos milk and identified the cholesterol degradation products by the bacterial cell. A small fraction of the enzyme synthesized by cells cultured in liquid medium for 7days was released into the medium whereas a larger fraction remained bound to the cell membrane. The extraction of this fraction was efficiently accomplished in 1 mM phosphate buffer, pH 7.0, containing 0.7% Triton X-100. The enzyme stability under freezing and at 45 o C was improved by addition of 20% glycerol. The optimum temperature and pH for the enzyme activity were 53°C and 7.5, respectively. The only steroidal product from cholesterol oxidation by the microbial cell and by the crude extract of the membrane-bound enzyme was 4-colesten-3-one. Chromatographic analysis showed that minor no steroidal compounds as well as 4-colesten-3-one found in the reaction media arose during fermentation process and were extracted together with the enzyme in the buffer solution. Cholesterol oxidation by the membrane-bound enzyme was a first order reaction type.

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Purification and characterization of extracellular 3.BETA.-hydroxysteroid oxidase produced by Streptoverticillium cholesterolicum.

Cited by 57 publications

References 0 publications

Hyperexpression and Analysis ofchoBEncoding Cholesterol Oxidase ofBrevibacterium sterolicuminEscherichia coliandStreptomyces lividans.

Hyperexpression and Analysis ofchoBEncoding Cholesterol Oxidase ofBrevibacterium sterolicuminEscherichia coliandStreptomyces lividans.

Nucleotide sequence of the gene for cholesterol oxidase from a Streptomyces sp

Some enzymatic properties of cholesterol oxidase produced by Brevibacterium sp

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