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Volumn 95, Issue 3, 2003, Pages 257-263

Purification and some properties of cholesterol oxidase stable in detergents from γ-proteobacterium Y-134

Author keywords

3 hydroxysteroid; Cholesterol oxidase; Detergent tolerant cholesterol oxidase; Thermostable cholesterol oxidase; Proteobacterium

Indexed keywords

ABSORPTION; DETERGENTS; ENZYMES;

EID: 0037265722     PISSN: 13891723     EISSN: None     Source Type: Journal    
DOI: 10.1263/jbb.95.257     Document Type: Article
Times cited : (22)

References (25)
  • 1
    • 85004503561 scopus 로고
    • Purification and some properties of cholesterol oxidases produced by an inducible and a constitutive mutant of Arthrobacter simplex
    • Liu, W-H., Meng, M-H., and Chen, K-S.: Purification and some properties of cholesterol oxidases produced by an inducible and a constitutive mutant of Arthrobacter simplex. Agric. Biol. Chem., 52, 413-418 (1988).
    • (1988) Agric. Biol. Chem. , vol.52 , pp. 413-418
    • Liu, W.-H.1    Meng, M.-H.2    Chen, K.-S.3
  • 2
    • 0016165542 scopus 로고
    • Properties of crystalline 3β-hydroxysteroid oxidase of Brevibacterium sterolicum
    • Uwajima, T., Yagi, H., and Terada, O.: Properties of crystalline 3β-hydroxysteroid oxidase of Brevibacterium sterolicum. Agric. Biol. Chem., 38, 1149-1156 (1974).
    • (1974) Agric. Biol. Chem. , vol.38 , pp. 1149-1156
    • Uwajima, T.1    Yagi, H.2    Terada, O.3
  • 3
    • 0001573065 scopus 로고
    • Purification and some properties of an extracellular 3β-hydroxysteroid oxidase produced by Corynebacterium cholesterolicum
    • Shirokane, Y., Nakamura, K., and Mizusawa, K.: Purification and some properties of an extracellular 3β-hydroxysteroid oxidase produced by Corynebacterium cholesterolicum. J. Ferment. Technol., 55, 337-346 (1977).
    • (1977) J. Ferment. Technol. , vol.55 , pp. 337-346
    • Shirokane, Y.1    Nakamura, K.2    Mizusawa, K.3
  • 4
    • 0019973014 scopus 로고
    • The characterization and interconversion of three forms of cholesterol oxidase extracted from Nocardia rhodochrous
    • Cheethan, P. S. J., Dunnill, P., and Lilly, M. D.: The characterization and interconversion of three forms of cholesterol oxidase extracted from Nocardia rhodochrous. Biochem. J., 201, 515-521 (1982).
    • (1982) Biochem. J. , vol.201 , pp. 515-521
    • Cheethan, P.S.J.1    Dunnill, P.2    Lilly, M.D.3
  • 5
    • 0001100909 scopus 로고
    • Purification and characterization of cholesterol oxidase from Pseudomonas sp. and taxonomic study of the strain
    • Lee, S-Y., Rhee, H-I., Tae, W-C., Shin, J-C., and Park, B-K.: Purification and characterization of cholesterol oxidase from Pseudomonas sp. and taxonomic study of the strain. Appl. Microbiol. Biotechnol., 31, 542-546 (1989).
    • (1989) Appl. Microbiol. Biotechnol. , vol.31 , pp. 542-546
    • Lee, S.-Y.1    Rhee, H.-I.2    Tae, W.-C.3    Shin, J.-C.4    Park, B.-K.5
  • 6
    • 0031805729 scopus 로고    scopus 로고
    • Purification of extracellular cholesterol oxidase with high activity in the presence of organic solvents from Pseudomonas sp. strain ST-200
    • Doukyu, N. and Aono, R.: Purification of extracellular cholesterol oxidase with high activity in the presence of organic solvents from Pseudomonas sp. strain ST-200. Appl. Environ. Microbiol., 64, 1929-1932 (1998).
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 1929-1932
    • Doukyu, N.1    Aono, R.2
  • 7
    • 0000032091 scopus 로고
    • Isolation of cholesterol oxidase from Rhodococcus equi ATCC 33706
    • Johnson, T. L. and Somkuti, G. A.: Isolation of cholesterol oxidase from Rhodococcus equi ATCC 33706. Biotechnol. Appl. Biochem., 13, 196-204 (1991).
    • (1991) Biotechnol. Appl. Biochem. , vol.13 , pp. 196-204
    • Johnson, T.L.1    Somkuti, G.A.2
  • 8
    • 0018399612 scopus 로고
    • Purification and some properties of cholesterol oxidase from Sehizophyllum commune with covalently bound flavin
    • Fukuyama, M. and Miyake, Y.: Purification and some properties of cholesterol oxidase from Sehizophyllum commune with covalently bound flavin. J. Biochem., 85, 1183-1193 (1979).
    • (1979) J. Biochem. , vol.85 , pp. 1183-1193
    • Fukuyama, M.1    Miyake, Y.2
  • 9
    • 0017125137 scopus 로고
    • Some enzymatic properties of 3β-hydroxysteroid oxidase produced by Streptomyces violascens
    • Tomioka, H., Kagawa, M., and Nakamura, S.: Some enzymatic properties of 3β-hydroxysteroid oxidase produced by Streptomyces violascens. J. Biochem., 79, 903-915 (1976).
    • (1976) J. Biochem. , vol.79 , pp. 903-915
    • Tomioka, H.1    Kagawa, M.2    Nakamura, S.3
  • 10
    • 85008023959 scopus 로고
    • Purification and characterization of extracellular 3β-hydroxysteroid oxidase produced by Streptoverticillium cholesterolicum
    • Inouye, Y., Taguchi, K., Fujii, A., Ishimaru, K., Nakamura, S., and Nomi, R.: Purification and characterization of extracellular 3β-hydroxysteroid oxidase produced by Streptoverticillium cholesterolicum. Chem. Pharm. Bull., 30, 951-958 (1982).
    • (1982) Chem. Pharm. Bull. , vol.30 , pp. 951-958
    • Inouye, Y.1    Taguchi, K.2    Fujii, A.3    Ishimaru, K.4    Nakamura, S.5    Nomi, R.6
  • 11
    • 0015719916 scopus 로고
    • Preparation and properties of a cholesterol oxidase from Nocardia sp. and its application to the enzymatic assay of total cholesterol in serum
    • Richmond, W.: Preparation and properties of a cholesterol oxidase from Nocardia sp. and its application to the enzymatic assay of total cholesterol in serum. Clin. Chem., 19, 1350-1356 (1973).
    • (1973) Clin. Chem. , vol.19 , pp. 1350-1356
    • Richmond, W.1
  • 13
    • 0028939982 scopus 로고
    • Direct measurement of high-density lipiprotein cholesterol in serum with polyethylene glycol-modified enzymes and sulfated α-cyclodextrin
    • Sugiuchi, H., Uji, Y., Okabe, H., Irie, T., Uekama, K., Kayahara, N., and Miyauchi, K.: Direct measurement of high-density lipiprotein cholesterol in serum with polyethylene glycol-modified enzymes and sulfated α-cyclodextrin. Clin. Chem., 41, 717-723 (1995).
    • (1995) Clin. Chem. , vol.41 , pp. 717-723
    • Sugiuchi, H.1    Uji, Y.2    Okabe, H.3    Irie, T.4    Uekama, K.5    Kayahara, N.6    Miyauchi, K.7
  • 14
    • 0032167791 scopus 로고    scopus 로고
    • Low-density lipoprotein cholesterol can be chemically measured: A new superior method
    • Okada, M., Mitsui, H., Ito, Y., Fujiwara, A., and Inao, K.: Low-density lipoprotein cholesterol can be chemically measured: a new superior method. J. Lab. Clin. Med., 132, 195-201 (1998).
    • (1998) J. Lab. Clin. Med. , vol.132 , pp. 195-201
    • Okada, M.1    Mitsui, H.2    Ito, Y.3    Fujiwara, A.4    Inao, K.5
  • 15
    • 0031887036 scopus 로고    scopus 로고
    • Homogenous assay for measuring low-density lipoprotein cholesterol in serum with triblock copolymer and α-cyclodextrin sulfate
    • Sugiuchi, H., Irie, T., Uji, Y., Ueno, T., Chaen, T., Uekama, K., and Okabe, H.: Homogenous assay for measuring low-density lipoprotein cholesterol in serum with triblock copolymer and α-cyclodextrin sulfate. Clin. Chem., 44, 522-531 (1998).
    • (1998) Clin. Chem. , vol.44 , pp. 522-531
    • Sugiuchi, H.1    Irie, T.2    Uji, Y.3    Ueno, T.4    Chaen, T.5    Uekama, K.6    Okabe, H.7
  • 16
    • 0017384270 scopus 로고
    • High density lipoprotein as a protective factor against coronary heart disease. The Framingham study
    • Gordon, T., Castelli, W. P., Hjortland, M. C., Kannel, W. B., and Dawber, T. R.: High density lipoprotein as a protective factor against coronary heart disease. The Framingham study. Am. J. Med., 62, 707-714 (1977).
    • (1977) Am. J. Med. , vol.62 , pp. 707-714
    • Gordon, T.1    Castelli, W.P.2    Hjortland, M.C.3    Kannel, W.B.4    Dawber, T.R.5
  • 17
    • 0019520249 scopus 로고
    • Lipoproteins, cardiovascular disease and death; the Framingham study
    • Gordon, T., Kannel, W. B., Castelli, W. P., and Dawber, T. R.: Lipoproteins, cardiovascular disease and death; the Framingham study. Arch. Intern. Med., 141, 1128-1131 (1981).
    • (1981) Arch. Intern. Med. , vol.141 , pp. 1128-1131
    • Gordon, T.1    Kannel, W.B.2    Castelli, W.P.3    Dawber, T.R.4
  • 18
    • 0034795345 scopus 로고    scopus 로고
    • Cloning, sequence analysis and expression of a gene encoding an organic solvent- and detergent-tolerant cholesterol oxidase of Burkholderia cepacia strain ST-200
    • Doukyu, N. and Aono, R.: Cloning, sequence analysis and expression of a gene encoding an organic solvent- and detergent-tolerant cholesterol oxidase of Burkholderia cepacia strain ST-200. Appl. Microbiol. Biotechnol., 57, 146-152 (2001).
    • (2001) Appl. Microbiol. Biotechnol. , vol.57 , pp. 146-152
    • Doukyu, N.1    Aono, R.2
  • 19
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson, J. D., Gibson, T. J., Plewniak, F., Jeanmougin, F., and Higgins, D. G.: The CLUSTAL X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res., 24, 4876-4882 (1997).
    • (1997) Nucleic Acids Res. , vol.24 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structure proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K.: Cleavage of structure proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685 (1970).
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0022381110 scopus 로고
    • Two new species of Pseudomonas. P. oryzihabitans isolated from rice paddy and clinical specimens and P. luteola isolated from clinical specimens
    • Komada, K., Kimura, N., and Komagata, K.: Two new species of Pseudomonas. P. oryzihabitans isolated from rice paddy and clinical specimens and P. luteola isolated from clinical specimens. Int. J. Syst. Bacteriol., 35, 467-474 (1985).
    • (1985) Int. J. Syst. Bacteriol. , vol.35 , pp. 467-474
    • Komada, K.1    Kimura, N.2    Komagata, K.3
  • 23
    • 0021840811 scopus 로고
    • Cellulolytic and dextranolytic gram-negative bacteria: Revival of the genus Cellvibrio
    • Blackall, L. L., Hayward, A. C., and Sly, L. I.: Cellulolytic and dextranolytic gram-negative bacteria: revival of the genus Cellvibrio. J. Appl. Bacteriol., 59, 81-97 (1985).
    • (1985) J. Appl. Bacteriol. , vol.59 , pp. 81-97
    • Blackall, L.L.1    Hayward, A.C.2    Sly, L.I.3
  • 24
    • 0024485646 scopus 로고
    • Nucleotide sequence of the gene for cholesterol oxidase from a Streptomyces sp.
    • Ishizaki, T., Hirayama, N., Shinkawa, H., Nimi, O., and Murooka, Y.: Nucleotide sequence of the gene for cholesterol oxidase from a Streptomyces sp. J. Bacteriol., 171, 596-601 (1989).
    • (1989) J. Bacteriol. , vol.171 , pp. 596-601
    • Ishizaki, T.1    Hirayama, N.2    Shinkawa, H.3    Nimi, O.4    Murooka, Y.5
  • 25
    • 0025745235 scopus 로고
    • Sequence of gene choB encoding cholesterol oxidase of Brevibacterium sterolicum: Comparison with choA of Streptomyces sp. SACOO
    • Ohta, T., Fujishiro, K., Yamaguchi, K., Tamura, Y., Aisaka, K., Uwajima, T., and Hasegawa, M.: Sequence of gene choB encoding cholesterol oxidase of Brevibacterium sterolicum: comparison with choA of Streptomyces sp. SACOO. Gene, 103, 93-96 (1991).
    • (1991) Gene , vol.103 , pp. 93-96
    • Ohta, T.1    Fujishiro, K.2    Yamaguchi, K.3    Tamura, Y.4    Aisaka, K.5    Uwajima, T.6    Hasegawa, M.7


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