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Volumn 152, Issue 2, 1997, Pages 209-216

The evidence of a laccase-like enzyme activity in a Bacillus sphaericus strain

Author keywords

Bacillus sphaericus; Laccase activity; Sporulation

Indexed keywords

BACILLUS SPHAERICUS; BACTERIA (MICROORGANISMS); FUNGI;

EID: 0030750335     PISSN: 09445013     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0944-5013(97)80014-6     Document Type: Article
Times cited : (76)

References (31)
  • 1
    • 0007178320 scopus 로고
    • Conversion of m-tyrosine to DOPA by a tyrosine hydroxylase from Bacillus cereus
    • Aronson J. N., Vicker R. S. (1965): Conversion of m-tyrosine to DOPA by a tyrosine hydroxylase from Bacillus cereus. Biochim. Biophys. Acta 110, 624-626.
    • (1965) Biochim. Biophys. Acta , vol.110 , pp. 624-626
    • Aronson, J.N.1    Vicker, R.S.2
  • 2
    • 0021180566 scopus 로고
    • Comparative studies of extracellular fungal laccases
    • Bollag J. M., Leonowicz A. (1984): Comparative studies of extracellular fungal laccases. Appl. Environ. Microbiol. 48, 849-854.
    • (1984) Appl. Environ. Microbiol. , vol.48 , pp. 849-854
    • Bollag, J.M.1    Leonowicz, A.2
  • 3
    • 0000400545 scopus 로고
    • The behaviour of phenoloxidases in the presence of clays and other soil-related adsorbents
    • Claus H., Filip Z. (1988): The behaviour of phenoloxidases in the presence of clays and other soil-related adsorbents. Appl. Microbiol. Biotechnol. 28, 506-511.
    • (1988) Appl. Microbiol. Biotechnol. , vol.28 , pp. 506-511
    • Claus, H.1    Filip, Z.2
  • 4
    • 0010668438 scopus 로고    scopus 로고
    • Microbial utilization and transformation of riverine humic substances
    • September 9-14, 1996, Wroclaw, Poland (in press)
    • Claus H., Filip Z., Alberts J. J. (1996): Microbial utilization and transformation of riverine humic substances. In: Proc. of the 8th Meeting Int. Humic Substances Society, September 9-14, 1996, Wroclaw, Poland (in press).
    • (1996) Proc. of the 8th Meeting Int. Humic Substances Society
    • Claus, H.1    Filip, Z.2    Alberts, J.J.3
  • 5
    • 0028928874 scopus 로고
    • Isolation of soil Streptomyces strains capable of degrading humic acids and analysis of their peroxidase activity
    • Dari K., Bechet M., Blondeau R. (1995): Isolation of soil Streptomyces strains capable of degrading humic acids and analysis of their peroxidase activity. FEMS Microbiol. Ecol. 16, 115-122.
    • (1995) FEMS Microbiol. Ecol. , vol.16 , pp. 115-122
    • Dari, K.1    Bechet, M.2    Blondeau, R.3
  • 6
    • 0344735710 scopus 로고
    • Laccase and the deposition of lignin in vascular plants
    • Dean J. F. D., Eriksson K. E. L (1994): Laccase and the deposition of lignin in vascular plants. Holzforsch. 48, 21-33.
    • (1994) Holzforsch. , vol.48 , pp. 21-33
    • Dean, J.F.D.1    Eriksson, K.E.L.2
  • 7
    • 0026637442 scopus 로고
    • Extracellular enzyme activities during humic acid degradation by the white rot fungi Phanerochaete chrysosporium and Trametes versicolor
    • Dehorter B., Blondeau R. (1992): Extracellular enzyme activities during humic acid degradation by the white rot fungi Phanerochaete chrysosporium and Trametes versicolor. FEMS Microbiol. Lett. 94, 209-216.
    • (1992) FEMS Microbiol. Lett. , vol.94 , pp. 209-216
    • Dehorter, B.1    Blondeau, R.2
  • 9
    • 0028954644 scopus 로고
    • Comparative study of substrates and inhibitors of Azospirillum lipoferum and Pyricularia oryzae laccases
    • Faure D., Bouillant M. L., Bally R. (1995): Comparative study of substrates and inhibitors of Azospirillum lipoferum and Pyricularia oryzae laccases. Appl. Environ. Microbiol. 61, 1144-1146.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 1144-1146
    • Faure, D.1    Bouillant, M.L.2    Bally, R.3
  • 10
    • 0012167560 scopus 로고    scopus 로고
    • Phenolic derivates related to lignin metabolism as substrates for Azospirillum laccase activity
    • Faure D., Bouillant M. L., Bally R. (1996): Phenolic derivates related to lignin metabolism as substrates for Azospirillum laccase activity. Phytochemistry 42, 357-360.
    • (1996) Phytochemistry , vol.42 , pp. 357-360
    • Faure, D.1    Bouillant, M.L.2    Bally, R.3
  • 11
    • 0002422670 scopus 로고
    • Effects of soil minerals on the formation of enzymes and their possible use in remediation of chemically polluted sites
    • (Eds.: Huang P. M., Berthelin J., Bollag J. M., McGill W. B., Page A. L.). CRC Press, Inc., Boca Raton
    • Filip Z., Claus H. (1995): Effects of soil minerals on the formation of enzymes and their possible use in remediation of chemically polluted sites. In : Environmental impacts of soil component interactions (Eds.: Huang P. M., Berthelin J., Bollag J. M., McGill W. B., Page A. L.). CRC Press, Inc., Boca Raton, 407-419.
    • (1995) Environmental Impacts of Soil Component Interactions , pp. 407-419
    • Filip, Z.1    Claus, H.2
  • 12
    • 0344504119 scopus 로고
    • Phenoloxidierende Enzyme - Ihre Eigenschaften und Wirkungen im Boden
    • Filip Z., Preusse T. (1985): Phenoloxidierende Enzyme - ihre Eigenschaften und Wirkungen im Boden. Pedobiologia 28, 133-142.
    • (1985) Pedobiologia , vol.28 , pp. 133-142
    • Filip, Z.1    Preusse, T.2
  • 13
    • 0002205562 scopus 로고
    • Differentiation of fungal tyrosinases and laccases using selective inhibitors and substrates
    • Enzymatic browning and ist prevention Washington
    • Flurkey W. H., Ratcliff B., Lopez L., Kuglin J., Dawley R. M. (1995): Differentiation of fungal tyrosinases and laccases using selective inhibitors and substrates. In: Enzymatic browning and ist prevention. American Chem. Soc. Symp. Ser. 600, Washington, 81-89.
    • (1995) American Chem. Soc. Symp. Ser. , vol.600 , pp. 81-89
    • Flurkey, W.H.1    Ratcliff, B.2    Lopez, L.3    Kuglin, J.4    Dawley, R.M.5
  • 14
    • 0027417556 scopus 로고
    • Polyphenol oxidase in Azospirillum lipoferum isolated from rice rhizosphere: Evidence for laccase activity in non-motile strains of Azospirillum lipoferum
    • Givaudan A., Effosse A., Faure D., Potier P., Bouillant M. L., Bally R. (1993): Polyphenol oxidase in Azospirillum lipoferum isolated from rice rhizosphere: evidence for laccase activity in non-motile strains of Azospirillum lipoferum. FEMS Microbiol. Lett. 108, 205-210.
    • (1993) FEMS Microbiol. Lett. , vol.108 , pp. 205-210
    • Givaudan, A.1    Effosse, A.2    Faure, D.3    Potier, P.4    Bouillant, M.L.5    Bally, R.6
  • 15
    • 0000910972 scopus 로고
    • Syringaldazine, an effective reagent for detecting laccase and peroxidase
    • Harkin J. M., Obst J. R. (1973): Syringaldazine, an effective reagent for detecting laccase and peroxidase. Experientia 29, 381-387.
    • (1973) Experientia , vol.29 , pp. 381-387
    • Harkin, J.M.1    Obst, J.R.2
  • 16
    • 0023467842 scopus 로고
    • Detection of peroxidase and its localisation in the forespore envelopes of Bacillus cereus
    • Ishida A. N., Futamura N., Matsusaka T. (1987): Detection of peroxidase and its localisation in the forespore envelopes of Bacillus cereus. J. Gen. Appl. Microbiol. 33, 27-32.
    • (1987) J. Gen. Appl. Microbiol. , vol.33 , pp. 27-32
    • Ishida, A.N.1    Futamura, N.2    Matsusaka, T.3
  • 17
    • 0012209328 scopus 로고
    • Laccase-like activity of nucleoside oxidase in the presence of nucleosides
    • Isono Y., Hoshino M. (1989): Laccase-like activity of nucleoside oxidase in the presence of nucleosides. Agric. Biol. Chem. 53, 2197-2203.
    • (1989) Agric. Biol. Chem. , vol.53 , pp. 2197-2203
    • Isono, Y.1    Hoshino, M.2
  • 18
    • 46549099510 scopus 로고
    • The inhibition of mushroom tyrosinase by tropolone
    • Kahn V., Andrawis A. (1985): The inhibition of mushroom tyrosinase by tropolone. Phytochemisty 24, 905-908.
    • (1985) Phytochemisty , vol.24 , pp. 905-908
    • Kahn, V.1    Andrawis, A.2
  • 19
    • 84986439430 scopus 로고
    • Effect of kojic acid on the oxidation of trihydroxyphenols by mushroom tyrosinase
    • Kahn V., Zakin V. (1995): Effect of kojic acid on the oxidation of trihydroxyphenols by mushroom tyrosinase. J. Food Biochem. 18, 427-443.
    • (1995) J. Food Biochem. , vol.18 , pp. 427-443
    • Kahn, V.1    Zakin, V.2
  • 20
    • 0014089703 scopus 로고
    • Determination of dipicolinic acid in bacterial spores by ultraviolet spectroscopy of the calcium chelate
    • Lewis J. C. (1967): Determination of dipicolinic acid in bacterial spores by ultraviolet spectroscopy of the calcium chelate. Anal. Biochem. 19, 327-337.
    • (1967) Anal. Biochem. , vol.19 , pp. 327-337
    • Lewis, J.C.1
  • 22
    • 46149132278 scopus 로고
    • Polyphenol oxidases in plants - Recent progress
    • Mayer A. M. (1987): Polyphenol oxidases in plants - recent progress. Phytochemisty 26, 111-20.
    • (1987) Phytochemisty , vol.26 , pp. 111-120
    • Mayer, A.M.1
  • 23
    • 85030298056 scopus 로고
    • Characteristics of tyrosinase in Bacillus subtilis
    • Mayles B. A. (1975): Characteristics of tyrosinase in Bacillus subtilis. Diss. Abstr. Int. B. 35, 5940-5941.
    • (1975) Diss. Abstr. Int. B. , vol.35 , pp. 5940-5941
    • Mayles, B.A.1
  • 24
    • 0001377614 scopus 로고
    • Oxidative coupling of aromatic compounds by enzymes from soil microorganisms
    • (Eds.: Paul E. A., Ladd J. N.) Marcel Dekker, Inc., New York
    • Sjoblad R. D., Bollag J. M. (1981): Oxidative coupling of aromatic compounds by enzymes from soil microorganisms. In: Soil Biochemistry (Eds.: Paul E. A., Ladd J. N.) vol. 5. Marcel Dekker, Inc., New York, 113-152.
    • (1981) Soil Biochemistry , vol.5 , pp. 113-152
    • Sjoblad, R.D.1    Bollag, J.M.2
  • 25
    • 0001411097 scopus 로고
    • Characterization of phosphatase in a terrestrial soil sterilized with an electron beam
    • Skujins J. J., Braal L., McLaren A. D. (1962): Characterization of phosphatase in a terrestrial soil sterilized with an electron beam. Enzymologia 25, 125-133.
    • (1962) Enzymologia , vol.25 , pp. 125-133
    • Skujins, J.J.1    Braal, L.2    McLaren, A.D.3
  • 26
    • 0028961640 scopus 로고
    • Production and characterization of laccase from Botrytis cineria 61-34
    • Slomcynski D., Nakas D., Tanenbaum S. W. (1995): Production and characterization of laccase from Botrytis cineria 61-34. Appl. Environ. Microbiol 61, 907-912.
    • (1995) Appl. Environ. Microbiol , vol.61 , pp. 907-912
    • Slomcynski, D.1    Nakas, D.2    Tanenbaum, S.W.3
  • 27
    • 0028766133 scopus 로고
    • Oxidation of humic substances by manganese oxides yields low-molecular-weight organic substrates
    • Sunda W. G., Kieber D. J. (1994): Oxidation of humic substances by manganese oxides yields low-molecular-weight organic substrates. Nature 367, 62-64.
    • (1994) Nature , vol.367 , pp. 62-64
    • Sunda, W.G.1    Kieber, D.J.2
  • 28
    • 0028013536 scopus 로고
    • The structure and function of fungal laccases
    • Thurston C. F. (1994): The structure and function of fungal laccases. Microbiol. 140, 19-26.
    • (1994) Microbiol. , vol.140 , pp. 19-26
    • Thurston, C.F.1
  • 29
    • 0029888257 scopus 로고    scopus 로고
    • Identification and characterization of a gene cluster involved in maganese oxidation by spores of the marine Bacillus sp. strain SG-1
    • van Waasbergen L. G., Hildebrand M., Tebo B. M. (1996): Identification and characterization of a gene cluster involved in maganese oxidation by spores of the marine Bacillus sp. strain SG-1. J. Bacteriol. 178, 3517-3530.
    • (1996) J. Bacteriol. , vol.178 , pp. 3517-3530
    • Van Waasbergen, L.G.1    Hildebrand, M.2    Tebo, B.M.3
  • 30
    • 0018943439 scopus 로고
    • Heat stability of Bacillus cereus enzymes in spores and in extracts
    • Warth A. D. (1980): Heat stability of Bacillus cereus enzymes in spores and in extracts. J. Bacteriol. 143, 27-34.
    • (1980) J. Bacteriol. , vol.143 , pp. 27-34
    • Warth, A.D.1
  • 31
    • 0027284683 scopus 로고
    • Cloning and characterization of genes encoding polypeptides present in the insoluble fraction of the spore coat of Bacillus subtilis
    • Zhang J., Fitz-James P. C., Aronson A. I. (1993): Cloning and characterization of genes encoding polypeptides present in the insoluble fraction of the spore coat of Bacillus subtilis. J. Bacteriol. 175, 3757-3766.
    • (1993) J. Bacteriol. , vol.175 , pp. 3757-3766
    • Zhang, J.1    Fitz-James, P.C.2    Aronson, A.I.3


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