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Volumn 160, Issue 3-4, 2012, Pages 161-168

Optimization of fermentation conditions for the production of human soluble catechol-O-methyltransferase by Escherichia coli using artificial neural network

Author keywords

Artificial neural networks; Catechol O metiltransferase; Escherichia coli; Experimental design; Fermentation

Indexed keywords

ARTIFICIAL NEURAL NETWORK MODELS; BIOPROCESSES; CATECHOL-O-METHYLTRANSFERASE; CATECHOL-O-METILTRANSFERASE; CENTRAL COMPOSITE DESIGNS; COMBINED EFFECT; COMPLEX MEDIUM; CULTURE MEDIA; FERMENTATION CONDITIONS; OPERATIONAL CONDITIONS; OPERATIONAL PARAMETERS; REGRESSION COEFFICIENT; STIRRING RATES;

EID: 84864071138     PISSN: 01681656     EISSN: 18734863     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2012.03.025     Document Type: Article
Times cited : (20)

References (27)
  • 1
    • 0030054732 scopus 로고    scopus 로고
    • How far are we in understanding the cause of Parkinson's disease?
    • Ben-Shlomo Y. How far are we in understanding the cause of Parkinson's disease?. Journal of Neurology, Neurosurgery and Psychiatry 1996, 61(1):4-16.
    • (1996) Journal of Neurology, Neurosurgery and Psychiatry , vol.61 , Issue.1 , pp. 4-16
    • Ben-Shlomo, Y.1
  • 2
    • 84872214871 scopus 로고    scopus 로고
    • Capture of rhPBGD from E. coli homogenate using EBA chromatography. Thesis LiTH-IFM-Ex-973. Sweden: Linköping University.
    • Björnsson P., 2001. Capture of rhPBGD from E. coli homogenate using EBA chromatography. Thesis LiTH-IFM-Ex-973. Sweden: Linköping University.
    • (2001)
    • Björnsson, P.1
  • 5
    • 8744311411 scopus 로고    scopus 로고
    • Quantitative screening of embryonic stem cell differentiation: endoderm formation as a model
    • Chang K.H., Zandstra P.W. Quantitative screening of embryonic stem cell differentiation: endoderm formation as a model. Biotechnology and Bioengineering 2004, 88:287-298.
    • (2004) Biotechnology and Bioengineering , vol.88 , pp. 287-298
    • Chang, K.H.1    Zandstra, P.W.2
  • 6
    • 79954990294 scopus 로고    scopus 로고
    • Artificial neural networks (ANN) approach for modeling of removal of Lanaset Red G on Chara contraria
    • Çelekli A., Geyik F. Artificial neural networks (ANN) approach for modeling of removal of Lanaset Red G on Chara contraria. Bioresource Technology 2011, 102(10):5634-5638.
    • (2011) Bioresource Technology , vol.102 , Issue.10 , pp. 5634-5638
    • Çelekli, A.1    Geyik, F.2
  • 8
    • 78651104124 scopus 로고    scopus 로고
    • Uniform stable-isotope labeling in mammalian cells: formulation of a cost-effective culture medium
    • Egorova-Zachernyuk T.A., Bosman G.J., Degrip W.J. Uniform stable-isotope labeling in mammalian cells: formulation of a cost-effective culture medium. Applied Microbiology and Biotechnology 2011, 89(2):397-406.
    • (2011) Applied Microbiology and Biotechnology , vol.89 , Issue.2 , pp. 397-406
    • Egorova-Zachernyuk, T.A.1    Bosman, G.J.2    Degrip, W.J.3
  • 9
    • 19944429270 scopus 로고    scopus 로고
    • Distinct geneexpression profiles in norepinephrine and epinephrine producing hereditary and sporadicpheochromocytomas: activation of hypoxia-driven angiogenic pathways in von Hippel-Lindau syndrome
    • Eisenhofer G., Huynh T-T., Pacak K., Brouwers F.M., Walther M.M., Linehan W.M., Munson P.J., Mannelli M., Goldstein D.S., Elkahloun A.G. Distinct geneexpression profiles in norepinephrine and epinephrine producing hereditary and sporadicpheochromocytomas: activation of hypoxia-driven angiogenic pathways in von Hippel-Lindau syndrome. Endocrine-Related Cancer 2004, 11(4):897-911.
    • (2004) Endocrine-Related Cancer , vol.11 , Issue.4 , pp. 897-911
    • Eisenhofer, G.1    Huynh, T.-T.2    Pacak, K.3    Brouwers, F.M.4    Walther, M.M.5    Linehan, W.M.6    Munson, P.J.7    Mannelli, M.8    Goldstein, D.S.9    Elkahloun, A.G.10
  • 11
    • 0029874193 scopus 로고    scopus 로고
    • High cell-density culture of Escherichia coli
    • Lee S.Y. High cell-density culture of Escherichia coli. Trends in Biotechnology 1996, 14:98-105.
    • (1996) Trends in Biotechnology , vol.14 , pp. 98-105
    • Lee, S.Y.1
  • 12
    • 54249109629 scopus 로고    scopus 로고
    • Review. Biocatalysts and bioreactor design
    • Mandenius C.F., Brundin A. Review. Biocatalysts and bioreactor design. Biotechnology Progress 2008, 24:1191-1203.
    • (2008) Biotechnology Progress , vol.24 , pp. 1191-1203
    • Mandenius, C.F.1    Brundin, A.2
  • 13
    • 70449103432 scopus 로고    scopus 로고
    • Effect of cosolvents on the structural stability of endoglucanase from Aspergillus aculeatus
    • Naika G.S., Prakash V., Tiku P.K. Effect of cosolvents on the structural stability of endoglucanase from Aspergillus aculeatus. Journal of Agriculture and Food Chemistry 2009, 57(21):10450-10456.
    • (2009) Journal of Agriculture and Food Chemistry , vol.57 , Issue.21 , pp. 10450-10456
    • Naika, G.S.1    Prakash, V.2    Tiku, P.K.3
  • 14
    • 33748951956 scopus 로고    scopus 로고
    • The effect of temperature on the analysis of metanephrine for catechol-O-methyltransferase activity assay by HPLC with electrochemical detection
    • Passarinha L.A., Bonifácio M.J., Queiroz J.A. The effect of temperature on the analysis of metanephrine for catechol-O-methyltransferase activity assay by HPLC with electrochemical detection. Biomedical Chromatography 2006, 20(9):937-944.
    • (2006) Biomedical Chromatography , vol.20 , Issue.9 , pp. 937-944
    • Passarinha, L.A.1    Bonifácio, M.J.2    Queiroz, J.A.3
  • 15
    • 37449015254 scopus 로고    scopus 로고
    • A new approach on the purification of recombinant human soluble catechol-O methyltransferase from an Escherichia coli extract using hydrophobic interaction chromatography
    • Passarinha L.A., Bonifácio M.J., Queiroz J.A. A new approach on the purification of recombinant human soluble catechol-O methyltransferase from an Escherichia coli extract using hydrophobic interaction chromatography. Journal of Chromatography A 2008, 1177:287-296.
    • (2008) Journal of Chromatography A , vol.1177 , pp. 287-296
    • Passarinha, L.A.1    Bonifácio, M.J.2    Queiroz, J.A.3
  • 16
    • 70849085440 scopus 로고    scopus 로고
    • Application of a fed-batch bioprocess for the heterologous production of hSCOMT in Escherichia coli
    • Passarinha L.A., Bonifácio M.J., Queiroz J.A. Application of a fed-batch bioprocess for the heterologous production of hSCOMT in Escherichia coli. Journal of Microbiology and Biotechnology 2009, 19(9):972-981.
    • (2009) Journal of Microbiology and Biotechnology , vol.19 , Issue.9 , pp. 972-981
    • Passarinha, L.A.1    Bonifácio, M.J.2    Queiroz, J.A.3
  • 17
    • 34249888727 scopus 로고    scopus 로고
    • Sequential optimization of culture medium composition for extracellular lipase production by Bacillus sphaericus using statistical methods
    • Rajendran A., Thangavelu V. Sequential optimization of culture medium composition for extracellular lipase production by Bacillus sphaericus using statistical methods. Journal of Chemical Technology and Biotechnology 2007, 82:460-470.
    • (2007) Journal of Chemical Technology and Biotechnology , vol.82 , pp. 460-470
    • Rajendran, A.1    Thangavelu, V.2
  • 18
  • 19
    • 84872210092 scopus 로고    scopus 로고
    • Optimizing the production of glucocorticoid receptor in insect cell-baculovirus expression system using response surface analysis. Thesis LiTH-IFM-Ex-980. Sweden, Linköping University.
    • Sävenhed, J. 2001. Optimizing the production of glucocorticoid receptor in insect cell-baculovirus expression system using response surface analysis. Thesis LiTH-IFM-Ex-980. Sweden, Linköping University.
    • (2001)
    • Sävenhed, J.1
  • 20
    • 59449096814 scopus 로고    scopus 로고
    • Optimization of actinomycin V production by Streptomyces triostinicus using artificial neural network and genetic algorithm
    • Singh V., Khan M., Khan S., Tripathi C.K.M. Optimization of actinomycin V production by Streptomyces triostinicus using artificial neural network and genetic algorithm. Applied Microbiology and Biotechnology 2009, 82:379-385.
    • (2009) Applied Microbiology and Biotechnology , vol.82 , pp. 379-385
    • Singh, V.1    Khan, M.2    Khan, S.3    Tripathi, C.K.M.4
  • 21
    • 47749090544 scopus 로고    scopus 로고
    • Artificial intelligence based optimization of exocellular glucansucrase production from Leuconostoc dextranicum NRRL B-1146
    • Singh A., Majumder A., Goyal A. Artificial intelligence based optimization of exocellular glucansucrase production from Leuconostoc dextranicum NRRL B-1146. Bioresource Technology 2008, 99(17):8201-8206.
    • (2008) Bioresource Technology , vol.99 , Issue.17 , pp. 8201-8206
    • Singh, A.1    Majumder, A.2    Goyal, A.3
  • 22
    • 0026752312 scopus 로고
    • Expression of recombinant soluble and membrane-bound catechol-O-methyltransferase in eukaryotic cells and identification of the respective enzymes in rat brain
    • Tilgmann C., Melen K., Lundström K., Jalanko A., Julkunen I., Kalkkinen N., Ulmanen I. Expression of recombinant soluble and membrane-bound catechol-O-methyltransferase in eukaryotic cells and identification of the respective enzymes in rat brain. European Journal of Biochemistry 1992, 207(2):813-821.
    • (1992) European Journal of Biochemistry , vol.207 , Issue.2 , pp. 813-821
    • Tilgmann, C.1    Melen, K.2    Lundström, K.3    Jalanko, A.4    Julkunen, I.5    Kalkkinen, N.6    Ulmanen, I.7
  • 23
    • 69249220246 scopus 로고    scopus 로고
    • Modeling of polygalacturonase enzyme activity and biomass production by Aspergillus sojae ATCC 20235
    • Tokatli F., Tari C., Unluturk S.M., Baysal N.G. Modeling of polygalacturonase enzyme activity and biomass production by Aspergillus sojae ATCC 20235. Journal of Industrial Microbiology & Biotechnology 2009, 36(9):1139-1148.
    • (2009) Journal of Industrial Microbiology & Biotechnology , vol.36 , Issue.9 , pp. 1139-1148
    • Tokatli, F.1    Tari, C.2    Unluturk, S.M.3    Baysal, N.G.4
  • 24
    • 0029175228 scopus 로고
    • Automatic laboratory-scale fed-batch procedure for production of recombinant proteins using inducible expression systems of Escherichia coli
    • Tomson K., Paalme T., Laakso P.S., Vilu R. Automatic laboratory-scale fed-batch procedure for production of recombinant proteins using inducible expression systems of Escherichia coli. Biotechnology Techniques 1995, 9(11):793-798.
    • (1995) Biotechnology Techniques , vol.9 , Issue.11 , pp. 793-798
    • Tomson, K.1    Paalme, T.2    Laakso, P.S.3    Vilu, R.4
  • 26
    • 0027199062 scopus 로고
    • Inhibition of the catechol-O-methyltransferase-catalyzed O-methylation of 2 and 4-hydroxyestradiol by catecholamine: implications for the mechanism of estrogen-induced carcinogenesis
    • Zhu B.T., Liehr J.G. Inhibition of the catechol-O-methyltransferase-catalyzed O-methylation of 2 and 4-hydroxyestradiol by catecholamine: implications for the mechanism of estrogen-induced carcinogenesis. Archives of Biochemistry and Biophysics 1993, 304(1):248-256.
    • (1993) Archives of Biochemistry and Biophysics , vol.304 , Issue.1 , pp. 248-256
    • Zhu, B.T.1    Liehr, J.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.