메뉴 건너뛰기




Volumn 99, Issue 4, 2008, Pages 699-702

Production of a thermostable uricase by a novel Bacillus thermocatenulatus strain

Author keywords

Bacillus thermocatenulatus; Cane molasses; Corn steep liquor; Uricase

Indexed keywords

BACTERIA; HEAT TREATMENT; MOLASSES; NITROGEN;

EID: 36049007136     PISSN: 09608524     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biortech.2007.01.048     Document Type: Article
Times cited : (47)

References (17)
  • 1
    • 13844299330 scopus 로고    scopus 로고
    • Improved production of Pseudomonas aeruginosa uricase by optimization of process parameters through statistical experimental designs
    • Abdel-Fattah Y.R., Saeed H.M., Gohar Y.M., and El-Baz M.A. Improved production of Pseudomonas aeruginosa uricase by optimization of process parameters through statistical experimental designs. Process Biochem. 40 (2005) 1707-1714
    • (2005) Process Biochem. , vol.40 , pp. 1707-1714
    • Abdel-Fattah, Y.R.1    Saeed, H.M.2    Gohar, Y.M.3    El-Baz, M.A.4
  • 2
    • 0034666315 scopus 로고    scopus 로고
    • Increased thermal resistance and modification of the catalytic properties of a β-glucosidase by random mutagenesis and in vitro recombination
    • Arrizubieta M.J., and Polaina J. Increased thermal resistance and modification of the catalytic properties of a β-glucosidase by random mutagenesis and in vitro recombination. J. Biol. Chem. 275 (2000) 28843-28848
    • (2000) J. Biol. Chem. , vol.275 , pp. 28843-28848
    • Arrizubieta, M.J.1    Polaina, J.2
  • 3
    • 0030663655 scopus 로고    scopus 로고
    • Crystal structure of the protein drug urate oxidase-inhibitor complex at 2.05 A resolution
    • Colloc'h N., Hajji M.E., Bachet B., L'Hermite G., Schiltz M., and Prange T. Crystal structure of the protein drug urate oxidase-inhibitor complex at 2.05 A resolution. Nat. Struct. Biol. 4 (1997) 947-952
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 947-952
    • Colloc'h, N.1    Hajji, M.E.2    Bachet, B.3    L'Hermite, G.4    Schiltz, M.5    Prange, T.6
  • 4
    • 0035868494 scopus 로고    scopus 로고
    • Identification and molecular characterization of a novel Bacillus strain capable of degrading Tween-80
    • El-Helow E.R. Identification and molecular characterization of a novel Bacillus strain capable of degrading Tween-80. FEMS Microbiol. Lett. 196 (2001) 119-122
    • (2001) FEMS Microbiol. Lett. , vol.196 , pp. 119-122
    • El-Helow, E.R.1
  • 5
    • 13844301726 scopus 로고
    • Uricase chungen zum bakteriellen purin uber den abbau von amino-, oxy-, und methylpurinen durch Pseudomonas aerogenousa (B. pyocyaneum)
    • Frank W., and Hahn G.E. Uricase chungen zum bakteriellen purin uber den abbau von amino-, oxy-, und methylpurinen durch Pseudomonas aerogenousa (B. pyocyaneum). Z. Physiol. Chem. 301 (1955) 90-106
    • (1955) Z. Physiol. Chem. , vol.301 , pp. 90-106
    • Frank, W.1    Hahn, G.E.2
  • 6
    • 0015165695 scopus 로고
    • Automated determination of uric acid, with use of a uricase-peroxidase system
    • Gochman N., and Schmitz M.J. Automated determination of uric acid, with use of a uricase-peroxidase system. Clin. Chem. 17 (1971) 1154-1159
    • (1971) Clin. Chem. , vol.17 , pp. 1154-1159
    • Gochman, N.1    Schmitz, M.J.2
  • 7
    • 0442310668 scopus 로고    scopus 로고
    • Modified colorimetric assay for uricase activity and a screen for mutant Bacillus subtilis uricase genes following StEP mutagenesis
    • Hunag S., and Wu T. Modified colorimetric assay for uricase activity and a screen for mutant Bacillus subtilis uricase genes following StEP mutagenesis. Eur. J. Biochem. 271 (2004) 517-523
    • (2004) Eur. J. Biochem. , vol.271 , pp. 517-523
    • Hunag, S.1    Wu, T.2
  • 9
    • 33751330608 scopus 로고
    • The determination of enzyme dissociation constants
    • Lineweaver H., and Burk D. The determination of enzyme dissociation constants. J. Am. Chem. Soc. 56 (1934) 658-666
    • (1934) J. Am. Chem. Soc. , vol.56 , pp. 658-666
    • Lineweaver, H.1    Burk, D.2
  • 10
    • 0019454713 scopus 로고
    • Purification and some properties of sarcosine oxidase from Corynebacterium sp. U-96
    • Masaru S. Purification and some properties of sarcosine oxidase from Corynebacterium sp. U-96. J. Biochem. 89 (1981) 599-607
    • (1981) J. Biochem. , vol.89 , pp. 599-607
    • Masaru, S.1
  • 11
    • 0033673176 scopus 로고    scopus 로고
    • Chemiluminometric determination of uric acid in plasma by closed-loop FIA with a coimmobilized enzyme flow cell
    • Nobutoshi K., Keisuke S., Takao M., Masaki T., Hitoshi K., and Kazue T. Chemiluminometric determination of uric acid in plasma by closed-loop FIA with a coimmobilized enzyme flow cell. Anal. Sci. 16 (2000) 1203-1205
    • (2000) Anal. Sci. , vol.16 , pp. 1203-1205
    • Nobutoshi, K.1    Keisuke, S.2    Takao, M.3    Masaki, T.4    Hitoshi, K.5    Kazue, T.6
  • 12
    • 0034010172 scopus 로고    scopus 로고
    • Comparative studies on citric acid production by Aspergillus niger and Candida lipolytica using molasses and glucose
    • Pazouki M., Felse P.A., Sinha J., and Panda T. Comparative studies on citric acid production by Aspergillus niger and Candida lipolytica using molasses and glucose. Bioproc. Eng. 22 (2000) 353-361
    • (2000) Bioproc. Eng. , vol.22 , pp. 353-361
    • Pazouki, M.1    Felse, P.A.2    Sinha, J.3    Panda, T.4
  • 13
    • 0031895304 scopus 로고    scopus 로고
    • High-level expression of the thermoalkalophilic lipase from Bacillus thermocatenulatus in Escherichia coli
    • Rua M.L., Atomi H., Schmidt-Dannert C., and Schmid R.D. High-level expression of the thermoalkalophilic lipase from Bacillus thermocatenulatus in Escherichia coli. Appl. Microbiol. Biotechnol. 49 (1998) 405-410
    • (1998) Appl. Microbiol. Biotechnol. , vol.49 , pp. 405-410
    • Rua, M.L.1    Atomi, H.2    Schmidt-Dannert, C.3    Schmid, R.D.4
  • 14
    • 0033841450 scopus 로고    scopus 로고
    • Therapeutic proteins: a comparison of chemical and biological properties of uricase conjugated to linear or branched poly (ethylene glycol) and poly (Nacryloylmorpholine)
    • Schiavon O., Caliceti P., Ferruti P., and Veronese F.M. Therapeutic proteins: a comparison of chemical and biological properties of uricase conjugated to linear or branched poly (ethylene glycol) and poly (Nacryloylmorpholine). Il Farmaco 55 (2000) 264-269
    • (2000) Il Farmaco , vol.55 , pp. 264-269
    • Schiavon, O.1    Caliceti, P.2    Ferruti, P.3    Veronese, F.M.4
  • 15
    • 0028025693 scopus 로고
    • Screening, purification and properties of a thermophilic lipase from Bacillus thermocatenulatus
    • Schmidt-Dannert C., Sztajer H., Stocklein W., Menge U., and Schmid R.D. Screening, purification and properties of a thermophilic lipase from Bacillus thermocatenulatus. Biochim. Biophys. Acta 1214 (1994) 43-53
    • (1994) Biochim. Biophys. Acta , vol.1214 , pp. 43-53
    • Schmidt-Dannert, C.1    Sztajer, H.2    Stocklein, W.3    Menge, U.4    Schmid, R.D.5
  • 16
    • 0016819581 scopus 로고
    • Purification and properties of xanthine dehydrogenase from Pseudomonas acidovorance
    • Sin I.L. Purification and properties of xanthine dehydrogenase from Pseudomonas acidovorance. Biochim. Biophys. Acta 410 (1975) 12-20
    • (1975) Biochim. Biophys. Acta , vol.410 , pp. 12-20
    • Sin, I.L.1
  • 17
    • 26844492591 scopus 로고    scopus 로고
    • Isolation of a thermostable uricase-producing bacterium and study on its enzyme production conditions
    • Zhou X., Ma X., Sun G., Li X., and Guo K. Isolation of a thermostable uricase-producing bacterium and study on its enzyme production conditions. Proc. Biochem. 40 (2005) 3749-3753
    • (2005) Proc. Biochem. , vol.40 , pp. 3749-3753
    • Zhou, X.1    Ma, X.2    Sun, G.3    Li, X.4    Guo, K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.