메뉴 건너뛰기




Volumn 23, Issue 3, 2007, Pages 645-651

High-level production of Bacillus subtilis glycine oxidase by fed-batch cultivation of recombinant Escherichia coli Rosetta (DE3)

Author keywords

[No Author keywords available]

Indexed keywords

EXPONENTIAL FEEDING; FED BATCH CULTIVATION; GLYCINE OXIDASE; SARCOSINE OXIDASE;

EID: 34250348784     PISSN: 87567938     EISSN: None     Source Type: Journal    
DOI: 10.1021/bp0603917     Document Type: Article
Times cited : (17)

References (28)
  • 1
    • 0025598210 scopus 로고
    • Continuous conversion to optically pure L-methionine from D-enantiomer contaminated preparations by an immobilized enzyme membrane reactor
    • Nakajima, N.; Conrad, D.; Sumi, H.; Suzuki, K.; Esaki, N.; Wandrey, C.; Soda, K. Continuous conversion to optically pure L-methionine from D-enantiomer contaminated preparations by an immobilized enzyme membrane reactor. J. Ferment. Technol. 1990, 70, 322-325.
    • (1990) J. Ferment. Technol , vol.70 , pp. 322-325
    • Nakajima, N.1    Conrad, D.2    Sumi, H.3    Suzuki, K.4    Esaki, N.5    Wandrey, C.6    Soda, K.7
  • 2
    • 0027523808 scopus 로고
    • Direct determination of the cephalosporin transforming activity of immobilized cells with use of an enzyme thermistor I Verification of the mathematical model
    • Gemeiner, P.; Stefuca, V.; Welwardova, A.; Michalkova, E.; Welward, L.; Kurillova, L.; Danielsson, B. Direct determination of the cephalosporin transforming activity of immobilized cells with use of an enzyme thermistor I Verification of the mathematical model. Enzyme Microb. Technol. 1993, 15, 50-56.
    • (1993) Enzyme Microb. Technol , vol.15 , pp. 50-56
    • Gemeiner, P.1    Stefuca, V.2    Welwardova, A.3    Michalkova, E.4    Welward, L.5    Kurillova, L.6    Danielsson, B.7
  • 3
    • 51249182938 scopus 로고
    • Production of α-keto acids. I. Immobilized cells of Trigonopsis variabilis containing D-amino acid oxidase
    • Brodelius, P.; Nilsson, K.; Mosbach, K. Production of α-keto acids. I. Immobilized cells of Trigonopsis variabilis containing D-amino acid oxidase. Appl. Biochem. Biotechnol. 1981, 6, 293-308.
    • (1981) Appl. Biochem. Biotechnol , vol.6 , pp. 293-308
    • Brodelius, P.1    Nilsson, K.2    Mosbach, K.3
  • 4
    • 0028665168 scopus 로고
    • Evaluation of D-amino acid oxidase from Rhodotorula gracilis for the production of α-keto acids: A reactor system
    • Butó, S.; Pollegioni, L.; D'Angiuro, L.; Pilone, M. S. Evaluation of D-amino acid oxidase from Rhodotorula gracilis for the production of α-keto acids: a reactor system. Biotechnol. Bioeng. 1994, 44, 1288-1294.
    • (1994) Biotechnol. Bioeng , vol.44 , pp. 1288-1294
    • Butó, S.1    Pollegioni, L.2    D'Angiuro, L.3    Pilone, M.S.4
  • 5
    • 0037010693 scopus 로고    scopus 로고
    • Minimization of by-product formation during D-amino acid oxidase catalyzed racemate resolution of D/L-amino acids
    • Trost, E. M.; Fischer, L. Minimization of by-product formation during D-amino acid oxidase catalyzed racemate resolution of D/L-amino acids. J. Mol. Catal. B 2002, 19-20, 189-195.
    • (2002) J. Mol. Catal. B , vol.19-20 , pp. 189-195
    • Trost, E.M.1    Fischer, L.2
  • 8
    • 0028960138 scopus 로고
    • A process for bioconversion of cephalosporin C by Rhodotorula gracilis D-amino acid oxidase
    • Pilone, M. S.; Buto, S.; Pollegioni, L. A process for bioconversion of cephalosporin C by Rhodotorula gracilis D-amino acid oxidase. Biotechnol. Lett. 1995, 17, 199-204.
    • (1995) Biotechnol. Lett , vol.17 , pp. 199-204
    • Pilone, M.S.1    Buto, S.2    Pollegioni, L.3
  • 9
    • 0000821303 scopus 로고
    • Stabilitation of D-amino acid oxidase from yeast Trigonopsis variabilis used for production of glutaryl-7-aminocephalosporanic acid from cephalosporanic C
    • Szwajcer-Dey, E.; Flygare, S.; Mosbach, K. Stabilitation of D-amino acid oxidase from yeast Trigonopsis variabilis used for production of glutaryl-7-aminocephalosporanic acid from cephalosporanic C. Appl. Biochem. Biotechnol. 1991, 27, 239-250.
    • (1991) Appl. Biochem. Biotechnol , vol.27 , pp. 239-250
    • Szwajcer-Dey, E.1    Flygare, S.2    Mosbach, K.3
  • 10
    • 0034307644 scopus 로고    scopus 로고
    • Expression of Trigonopsis variabilis D-amino acid oxidase gene in Escherichia coli and characterization of its inactive mutants
    • Lin, L. L.; Chien, H. R.; Wang, W. C.; Hwang, T. S.; Fu, H. M.; Hsu, W. H. Expression of Trigonopsis variabilis D-amino acid oxidase gene in Escherichia coli and characterization of its inactive mutants. Enzyme Microb. Technol. 2000, 27, 482-491.
    • (2000) Enzyme Microb. Technol , vol.27 , pp. 482-491
    • Lin, L.L.1    Chien, H.R.2    Wang, W.C.3    Hwang, T.S.4    Fu, H.M.5    Hsu, W.H.6
  • 11
    • 0036125060 scopus 로고    scopus 로고
    • Overexpression of a recombinant wild-type and His-tagged Bacillus subtilis glycine oxidase in Escherichia coli
    • Job, V.; Molla, G.; Pilone, M. S.; Pollegioni, L. Overexpression of a recombinant wild-type and His-tagged Bacillus subtilis glycine oxidase in Escherichia coli. Eur. J. Biochem. 2002a, 269, 1456-1463.
    • (2002) Eur. J. Biochem , vol.269 , pp. 1456-1463
    • Job, V.1    Molla, G.2    Pilone, M.S.3    Pollegioni, L.4
  • 12
    • 0031737874 scopus 로고    scopus 로고
    • Purification and characterization of a novel glycine oxidase from Bacillus subtilis
    • Nishiya, Y.; Imanaka, T. Purification and characterization of a novel glycine oxidase from Bacillus subtilis. FEBS Lett. 1998, 438, 263-266.
    • (1998) FEBS Lett , vol.438 , pp. 263-266
    • Nishiya, Y.1    Imanaka, T.2
  • 14
    • 0037452907 scopus 로고    scopus 로고
    • Structural and mechanistic studies on ThiO, a glycine oxidase essential for thiamine biosynthesis in Bacillus subtilis
    • Settembre, E. C.; Dorrestein, P. C.; Park, J. H.; Augustine, A. M.; Begley, T. P.; Ealick, S. E. Structural and mechanistic studies on ThiO, a glycine oxidase essential for thiamine biosynthesis in Bacillus subtilis. Biochemistry 2003, 42, 2971-2981.
    • (2003) Biochemistry , vol.42 , pp. 2971-2981
    • Settembre, E.C.1    Dorrestein, P.C.2    Park, J.H.3    Augustine, A.M.4    Begley, T.P.5    Ealick, S.E.6
  • 18
    • 85083232435 scopus 로고    scopus 로고
    • Peuker, T.; Ellert, A.; Kaiser, C.; Lenz, K.; Elsholz, O.; Luttmann, R. On-line monitoring of physiological parameters in High Cell Density Cultivations with Escherichia coli. In 9th IFAC International Symposium on Computer Applications in Biotechnology; Pons, M. N., v Impe, J. F. M., Eds.; Elsevier Proceedings: Nancy, France, 2004; pp 333-338.
    • Peuker, T.; Ellert, A.; Kaiser, C.; Lenz, K.; Elsholz, O.; Luttmann, R. On-line monitoring of physiological parameters in High Cell Density Cultivations with Escherichia coli. In 9th IFAC International Symposium on Computer Applications in Biotechnology; Pons, M. N., v Impe, J. F. M., Eds.; Elsevier Proceedings: Nancy, France, 2004; pp 333-338.
  • 20
    • 33745601275 scopus 로고    scopus 로고
    • Control development of bioreactor process with online simulation methods
    • Schügerl, K, Bellgardt, K. H, Eds, Springer: Berlin
    • Luttmann, R.; Gollmer, K. Control development of bioreactor process with online simulation methods. In Bioreaction Engineering; Schügerl, K., Bellgardt, K. H., Eds.; Springer: Berlin, 2000; Vol. 4.
    • (2000) Bioreaction Engineering , vol.4
    • Luttmann, R.1    Gollmer, K.2
  • 21
    • 0014478342 scopus 로고
    • Determination of blood glucose using an oxidase-peroxidase system with a non-carcinogenic chromogen
    • Trinder, P. Determination of blood glucose using an oxidase-peroxidase system with a non-carcinogenic chromogen. J. Clin. Pathol. 1969, 22, 158-161.
    • (1969) J. Clin. Pathol , vol.22 , pp. 158-161
    • Trinder, P.1
  • 22
    • 7444235940 scopus 로고    scopus 로고
    • Fed-batch production of recombinant fuculose-1-phosphate aldolase in E coli
    • Durany, O.; de Mas, C.; López-Santín, J. Fed-batch production of recombinant fuculose-1-phosphate aldolase in E coli. Process. Biochem. 2005, 40, 707-716.
    • (2005) Process. Biochem , vol.40 , pp. 707-716
    • Durany, O.1    de Mas, C.2    López-Santín, J.3
  • 23
    • 0344242080 scopus 로고    scopus 로고
    • High-level production of human leptin by fed-batch cultivation of recombinant Escherichia coli and its purification
    • Jeong, K. J.; Lee, S. Y. High-level production of human leptin by fed-batch cultivation of recombinant Escherichia coli and its purification. Appl. Environ. Microbiol. 1999, 65, 3027-3032.
    • (1999) Appl. Environ. Microbiol , vol.65 , pp. 3027-3032
    • Jeong, K.J.1    Lee, S.Y.2
  • 24
    • 0033935592 scopus 로고    scopus 로고
    • Efficient secretory production of alkaline phosphatase by high cell density culture of recombinant Escherichia coli using Bacillus sp endoxylanase signal sequence
    • Choi, J. H.; Jeong, K. J., Kim, S. C.; Lee, S. Y. Efficient secretory production of alkaline phosphatase by high cell density culture of recombinant Escherichia coli using Bacillus sp endoxylanase signal sequence. Appl. Microbiol. Biotechnol. 2000, 53, 640-645.
    • (2000) Appl. Microbiol. Biotechnol , vol.53 , pp. 640-645
    • Choi, J.H.1    Jeong, K.J.2    Kim, S.C.3    Lee, S.Y.4
  • 25
    • 2442704008 scopus 로고    scopus 로고
    • High cell density fed-batch cultivation of Escherichia coli using exponential feeding combined with pH-stat
    • Kim, B. S.; Lee, S. C.; Lee, S. Y.; Chang, Y. K.; Chang, H. N. High cell density fed-batch cultivation of Escherichia coli using exponential feeding combined with pH-stat. Bioprocess Biosyst. Eng. 2004, 26, 147-150.
    • (2004) Bioprocess Biosyst. Eng , vol.26 , pp. 147-150
    • Kim, B.S.1    Lee, S.C.2    Lee, S.Y.3    Chang, Y.K.4    Chang, H.N.5
  • 26
    • 8044237717 scopus 로고    scopus 로고
    • High volumetric yields of functional dimeric miniantibodies in Escherichia coli, using an optimized expression vector and high-cell-density fermentation under non-limited growth conditions
    • Horn, U.; Strittmatter, A.; Krebber, A.; Knüpfer, U.; Kujau, M.; Wenderoth, R.; Müller, K.; Matzku, S.; Pluckthun, A.; Riesenberg, D. High volumetric yields of functional dimeric miniantibodies in Escherichia coli, using an optimized expression vector and high-cell-density fermentation under non-limited growth conditions. Appl. Microbiol. Biotechnol. 1996, 46, 524-532.
    • (1996) Appl. Microbiol. Biotechnol , vol.46 , pp. 524-532
    • Horn, U.1    Strittmatter, A.2    Krebber, A.3    Knüpfer, U.4    Kujau, M.5    Wenderoth, R.6    Müller, K.7    Matzku, S.8    Pluckthun, A.9    Riesenberg, D.10
  • 27
    • 0035660851 scopus 로고    scopus 로고
    • High-level secretory production of human granulocyte-colony stimulating factor by fed-batch culture of recombinant Escherichia coli
    • Yim, S. C.; Jeong, K. J.; Chang, H. N.; Lee, S. Y. High-level secretory production of human granulocyte-colony stimulating factor by fed-batch culture of recombinant Escherichia coli. Bioprocess Biosyst. Eng. 2001, 24, 249-254.
    • (2001) Bioprocess Biosyst. Eng , vol.24 , pp. 249-254
    • Yim, S.C.1    Jeong, K.J.2    Chang, H.N.3    Lee, S.Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.