메뉴 건너뛰기




Volumn 104, Issue 1, 2009, Pages 134-142

Step change in the efficiency of centrifugation through cell engineering: Co-expression of Staphylococcal nuclease to reduce the viscosity of the bioprocess feedstock

Author keywords

Cell disruption; Cell engineering; Clarification; Nuclease; Viscosity

Indexed keywords

BIOPROCESSES; BIOPROCESSINGS; CELL DEBRIS; CELL DISRUPTION; CELL ENGINEERING; CLARIFICATION PERFORMANCE; CO-EXPRESSION; DOWNSTREAM-PROCESSING; E. COLI; LABORATORY SCALE; NUCLEASE; PROCESS STREAMS; RECOMBINANT PROTEIN; SCALE-DOWN; STAPHYLOCOCCAL NUCLEASE; STAPHYLOCOCCUS AUREUS; STEP CHANGES; VISCOSITY REDUCTION;

EID: 67650692398     PISSN: 00063592     EISSN: 10970290     Source Type: Journal    
DOI: 10.1002/bit.22369     Document Type: Article
Times cited : (29)

References (45)
  • 1
    • 0025639149 scopus 로고
    • Characterization of E. coli cell disintegrates from a bead mill and high pressure homogenizers
    • Agerkvist I, Enfors S-O. 1990. Characterization of E. coli cell disintegrates from a bead mill and high pressure homogenizers. Biotechnol Bioeng 36:1083-1089.
    • (1990) Biotechnol Bioeng , vol.36 , pp. 1083-1089
    • Agerkvist, I.1    Enfors, S.-O.2
  • 3
    • 4644309963 scopus 로고    scopus 로고
    • Production technologies for monoclonal antibodies and their fragments
    • DOI 10.1016/j.copbio.2004.08.002, PII S0958166904001089
    • Andersen DC, Reilly DE. 2004. Production technologies for monoclonal antibodies and their fragments. Curr Opin Biotechnol 15:456-462. (Pubitemid 39304044)
    • (2004) Current Opinion in Biotechnology , vol.15 , Issue.5 , pp. 456-462
    • Andersen, D.C.1    Reilly, D.E.2
  • 4
    • 77956899130 scopus 로고
    • Staphylococcal nuclease, chemical properties and catalysis
    • Boyer P, editor New York: Academic Press
    • Anfinsen CB, Cuatrecasas P, Taniuchi H. 1971. Staphylococcal nuclease, chemical properties and catalysis. In: Boyer P, editor. The enzymes, Vol.4. New York: Academic Press, p 177-204.
    • (1971) The Enzymes , vol.4 , pp. 177-204
    • Anfinsen, C.B.1    Cuatrecasas, P.2    Taniuchi, H.3
  • 6
    • 0004270170 scopus 로고
    • Ausubel FM, Brent R, Kingston RE, Moore DD, Seidman JG, Smith JA, Struhl K, editors New York: Greene Publishing Associates and Wiley-Interscience, 2.1.3-2.1.4, 15.3.8-15.3.11p
    • Ausubel FM, Brent R, Kingston RE, Moore DD, Seidman JG, Smith JA, Struhl K, editors. 1987. Current protocols in molecular biology. New York: Greene Publishing Associates and Wiley-Interscience, 2.1.3-2.1.4, 15.3.8-15.3.11p.
    • (1987) Current Protocols in Molecular Biology
  • 7
    • 0002739483 scopus 로고    scopus 로고
    • Derivatives and genotypes of some mutant derivatives of Escherichia coli K-12
    • Neidhardt FC, et al. editors Washington: ASM Press
    • Bachmann BJ. 1996. Derivatives and genotypes of some mutant derivatives of Escherichia coli K-12. In: Neidhardt FC, et al. editors. Escherichia coli and Salmonella: Cellular and molecular biology, 2nd edn. Washington: ASM Press, p 2460-2488.
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology, 2nd Edn , pp. 2460-2488
    • Bachmann, B.J.1
  • 8
    • 0031555168 scopus 로고    scopus 로고
    • Crossflow microfiltration of recombinant Escherichia coli lysates after high pressure homogenization
    • Bailey SM, Meagher MM. 1997. Crossflow microfiltration of recombinant Escherichia coli lysates after high pressure homogenization. Biotechnol Bioeng 56:304-310.
    • (1997) Biotechnol Bioeng , vol.56 , pp. 304-310
    • Bailey, S.M.1    Meagher, M.M.2
  • 9
    • 0029360382 scopus 로고
    • Improved homogenization of recombinant Escherichia coli following pretreatment with guanidine hydrochloride
    • Bailey SM, Blum P, Meagher MM. 1995. Improved homogenization of recombinant Escherichia coli following pretreatment with guanidine hydrochloride. Biotechnol Prog 11:533-539.
    • (1995) Biotechnol Prog , vol.11 , pp. 533-539
    • Bailey, S.M.1    Blum, P.2    Meagher, M.M.3
  • 10
    • 0023470603 scopus 로고
    • The extracellular nuclease gene of Serratia marcescens and its secretion from Escherichia coli
    • Ball TK, Saurugger PN, Benedik MJ. 1987. The extracellular nuclease gene of Serratia marcescens and its secretion from Escherichia coli. Gene 57:183-192.
    • (1987) Gene , vol.57 , pp. 183-192
    • Ball, T.K.1    Saurugger, P.N.2    Benedik, M.J.3
  • 11
    • 0034609030 scopus 로고    scopus 로고
    • Laboratory scaledown of protein purification processes involving fractional precipitation and centrifugal recovery
    • Boychyn M, Doyle W, Bulmer M, More J, Hoare M. 2000. Laboratory scaledown of protein purification processes involving fractional precipitation and centrifugal recovery. Biotechnol Bioeng 69:1-10. (Pubitemid 30418256)
    • (2000) Biotechnology and Bioengineering , vol.69 , Issue.1 , pp. 1-10
    • Boychyn, M.1    Doyle, W.2    Bulmer, M.3    More, J.4    Hoare, M.5
  • 14
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 16
    • 0037457421 scopus 로고    scopus 로고
    • A modified Escherichia coli protein production strain expressing staphylococcal nuclease, capable of auto-hydrolysing host nucleic acid
    • Cooke GD, Cranenburgh RM, Hanak JAJ, Ward JM. 2003. A modified Escherichia coli protein production strain expressing staphylococcal nuclease, capable of auto-hydrolysing host nucleic acid. J Biotechnol 101:229-239.
    • (2003) J Biotechnol , vol.101 , pp. 229-239
    • Cooke, G.D.1    Cranenburgh, R.M.2    Hanak, J.A.J.3    Ward, J.M.4
  • 17
    • 0023312664 scopus 로고
    • CENTRIFUGAL SEPARATION in the RECOVERY of INTRACELLULAR PROTEIN from E. COLI
    • DOI 10.1016/0300-9467(87)85021-9
    • Datar R, Rosen CG. 1987. Centrifugal separation in the recovery of intracellular protein from E. coli. Chem Eng J 34:B49-B56. (Pubitemid 17572199)
    • (1987) Chemical Engineering Journal , vol.34 , Issue.3
    • Datar, R.1    Rosen, C.-G.2
  • 19
    • 0003308802 scopus 로고
    • Membrane systems
    • Asenjo JA, editor New York; Basel: Marcel Dekker, Inc.
    • Fane AG, Radovich GM. 1990. Membrane systems. In: Asenjo JA, editor. Separation processes in biotechnology. New York; Basel: Marcel Dekker, Inc., p 209-262.
    • (1990) Separation Processes in Biotechnology , pp. 209-262
    • Fane, A.G.1    Radovich, G.M.2
  • 20
    • 0028483113 scopus 로고
    • Pilot scale recovery of recombinant annexin V from unclarified Escherichia coli homogenate using expanded bed adsorption
    • DOI 10.1002/bit.260440808
    • Frej AKB, Hjorth R, Hammarstrom A. 1994. Pilot scale recovery of recombinant annexin V from unclarified Escherichia coli homogenate using expanded bed adsorption. Biotechnol Bioeng 44:922. (Pubitemid 24308540)
    • (1994) Biotechnology and Bioengineering , vol.44 , Issue.8 , pp. 922-929
    • Barnfield Frej, A.K.1    Hjorth, R.2    Hammarstrom, A.3
  • 21
    • 0022870839 scopus 로고
    • Molecular cloning of the plasmid RP4 primase region in a multi-host-range tacP expression vector
    • DOI 10.1016/0378-1119(86)90358-6
    • Furste JP, Pansegrau W, Frank R, Blcker H, Scholz P, Bagdasarian M, Lanka E. 1986. Molecular cloning of the plasmid RP4 primase region in a multi-host-range tacP expression vector. Gene 48:119-131. (Pubitemid 17006084)
    • (1986) Gene , vol.48 , Issue.1 , pp. 119-131
    • Furste, J.P.1    Pansegrau, W.2    Frank, R.3
  • 22
    • 67349150622 scopus 로고    scopus 로고
    • BugBuster™ and Benzonase®: The clear solutions to simple efficient extraction of E. coli proteins
    • Grabski A, McCormick M, Mierendorf O. 1999. BugBuster™ and Benzonase®: The clear solutions to simple efficient extraction of E. coli proteins. Innovations 10:17-19.
    • (1999) Innovations , vol.10 , pp. 17-19
    • Grabski, A.1    McCormick, M.2    Mierendorf, O.3
  • 23
    • 0030131710 scopus 로고    scopus 로고
    • Optimization of poly(ethylene glycol) precipitation of hepatitis a virus used to prepare a highly purified inactivated vaccine
    • Hagen AJ, Oliver CN, Sitrin RD. 1996. Optimization of poly(ethylene glycol) precipitation of hepatitis A virus used to prepare a highly purified inactivated vaccine. Biotechnol Prog 12:406-412.
    • (1996) Biotechnol Prog , vol.12 , pp. 406-412
    • Hagen, A.J.1    Oliver, C.N.2    Sitrin, R.D.3
  • 24
    • 0035967452 scopus 로고    scopus 로고
    • Particle movement in non-Newtonian slurries: The effect of yield stress on dense medium separation
    • DOI 10.1016/S0009-2509(00)00479-6, PII S0009250900004796, Collection of papers presented at the Eigth Nisshin Engineering Particle Technology International Seminar
    • He YB, Laskowski JS, Klein B. 2001. Particle movement in non-Newtonian slurries: The effect of yield stress on dense medium separation. Chem Eng Sci 56:2991-2998. (Pubitemid 32548519)
    • (2001) Chemical Engineering Science , vol.56 , Issue.9 , pp. 2991-2998
    • He, Y.B.1    Laskowski, J.S.2    Klein, B.3
  • 25
    • 0020097844 scopus 로고
    • Protein precipitation and precipitate ageing
    • Hoare M. 1982. Protein precipitation and precipitate ageing. Trans Inst Chem Eng 60:79-87.
    • (1982) Trans Inst Chem Eng , vol.60 , pp. 79-87
    • Hoare, M.1
  • 26
    • 3543081058 scopus 로고    scopus 로고
    • Engineering of Escherichia coli to improve the purification of periplasmic Fab? fragments: Changing the pI of the chromosomally encoded PhoS/PstS protein
    • Humphreys DP, Heywood SP, King LM, Bowering LC, Turner JP, Lane SE. 2004. Engineering of Escherichia coli to improve the purification of periplasmic Fab? fragments: Changing the pI of the chromosomally encoded PhoS/PstS protein. Protein Expression Purif 37:109-118.
    • (2004) Protein Expression Purif , vol.37 , pp. 109-118
    • Humphreys, D.P.1    Heywood, S.P.2    King, L.M.3    Bowering, L.C.4    Turner, J.P.5    Lane, S.E.6
  • 27
    • 33749364369 scopus 로고    scopus 로고
    • Shear stress analysis of mammalian cell suspensions for prediction of industrial centrifugation and its verification
    • DOI 10.1002/bit.21029
    • Hutchinson N, Bingham N, Murrell N, Farid S, Hoare M. 2006. Shear stress analysis of mammalian cell suspensions for prediction of industrial centrifugation and its verification. Biotechnol Bioeng 95:483-491. (Pubitemid 44495383)
    • (2006) Biotechnology and Bioengineering , vol.95 , Issue.3 , pp. 483-491
    • Hutchinson, N.1    Bingham, N.2    Murrell, N.3    Farid, S.4    Hoare, M.5
  • 29
    • 2442542108 scopus 로고
    • New findings on fundamentals of cell disruption in high pressure homogenisers
    • White MD, Reuveny S, Shafferman A, editors Weinheim: Balaban publishers
    • Keshavarz E. 1991. New findings on fundamentals of cell disruption in high pressure homogenisers. In: White MD, Reuveny S, Shafferman A, editors. Biologicals from recombinant microorganisms and animal cells production and recovery. Weinheim: Balaban publishers, p 277-292.
    • (1991) Biologicals from Recombinant Microorganisms and Animal Cells Production and Recovery , pp. 277-292
    • Keshavarz, E.1
  • 30
    • 0025455983 scopus 로고
    • Disruption of a fungal organism, rhizopus nigricans, in a high-pressure homogenizer
    • DOI 10.1016/0141-0229(90)90064-W
    • Keshavarz E, Bonnerjea J, Hoare M, Dunnill P. 1990. Disruption of a fungal organism, Rhizopus nigricans, in a high-pressure homogenizer. Enz Microb Technol 12:494-498. (Pubitemid 20331658)
    • (1990) Enzyme and Microbial Technology , vol.12 , Issue.7 , pp. 494-498
    • Keshavarz, E.1    Bonnerjea, J.2    Hoare, M.3    Dunnill, P.4
  • 32
    • 0347761244 scopus 로고    scopus 로고
    • Combined In-Fermenter Extraction and Cross-Flow Microfiltration for Improved Inclusion Body Processing
    • DOI 10.1002/bit.10878
    • Lee CT, Morreale G, Middelberg APJ. 2004. Combined in-fermenter extraction and cross-flow microfiltration for improved inclusion body processing. Biotechnol Bioeng 85:103-113. (Pubitemid 38090135)
    • (2004) Biotechnology and Bioengineering , vol.85 , Issue.1 , pp. 103-113
    • Lee, C.T.1    Morreale, G.2    Middelberg, A.P.J.3
  • 35
    • 0037454676 scopus 로고    scopus 로고
    • Ultra scale-down approach for the prediction of full-scale recovery of ovine polycolonal immunoglobulins used in the manufacture of snake venom-specific fab fragment
    • DOI 10.1002/bit.10454
    • Neal G, Christie J, Ayazi-Shamlou P, Keshavarz-Moore E. 2003. An ultra scale-down approach for the prediction of full-scale recovery of ovine polyclonal immunoglobulins used in the manufacture of snake venomspecific Fab? fragment. Biotechnol Bioeng 81:149-157. (Pubitemid 36077291)
    • (2003) Biotechnology and Bioengineering , vol.81 , Issue.2 , pp. 149-157
    • Neal, G.1    Christie, J.2    Keshavarz-Moore, E.3    Shamlou, P.A.4
  • 36
    • 4744342353 scopus 로고    scopus 로고
    • Alternative bioseparation operations: Life beyond packed-bed chromatography
    • Przybycien TM, Pujar NS, Steele LM. 2004. Alternative bioseparation operations: Life beyond packed-bed chromatography. Curr Opin Biotechnol 15:469-478.
    • (2004) Curr Opin Biotechnol , vol.15 , pp. 469-478
    • Przybycien, T.M.1    Pujar, N.S.2    Steele, L.M.3
  • 37
    • 0035204202 scopus 로고    scopus 로고
    • Comparative biology of IncQ and IncQ-like plasmids
    • DOI 10.1128/MMBR.65.4.481-496.2001
    • Rawlings DE, Tietze E. 2001. Comparative biology of IncQ and IncQ-like plasmids. Microbiol Mol Biol Rev 65:481-496. (Pubitemid 33123515)
    • (2001) Microbiology and Molecular Biology Reviews , vol.65 , Issue.4 , pp. 481-496
    • Rawlings, D.E.1    Tietze, E.2
  • 38
    • 33845409018 scopus 로고    scopus 로고
    • A methodology for centrifuge selection for the separation of high solids density cell broths by visualisation of performance using windows of operation
    • DOI 10.1002/bit.21102
    • Salte H, King JM, Baganz F, Hoare M, Titchener-Hooker NJ. 2006. A methodology for centrifuge selection for the separation of high solids density cell broths by visualisation of performance using windows of operation. Biotechnol Bioeng 95:1218-1227. (Pubitemid 44901337)
    • (2006) Biotechnology and Bioengineering , vol.95 , Issue.6 , pp. 1218-1227
    • Salte, H.1    King, J.M.P.2    Baganz, F.3    Hoare, M.4    Titchener-Hooker, N.J.5
  • 39
    • 0024106674 scopus 로고
    • Effect of solution viscosity on ultrafiltration flux
    • Shu-Sen W. 1988. Effect of solution viscosity on ultrafiltration flux. J Membr Sci 39:187-194.
    • (1988) J Membr Sci , vol.39 , pp. 187-194
    • Shu-Sen, W.1
  • 40
    • 0030130780 scopus 로고    scopus 로고
    • Simulation of particle size distribution changes occurring during high- Pressure disruption of bakers' yeast
    • DOI 10.1002/(SICI)1097-0290(19960420)50:2<145::AID-BIT4>3.0.CO;2-M
    • Siddiqi SF, Titchener-Hooker NJ, Shamlou A. 1996. Simulation of particle size distribution changes occurring during high-pressure disruption of bakers? yeast. Biotechnol Bioeng 50:145-150. (Pubitemid 26095148)
    • (1996) Biotechnology and Bioengineering , vol.50 , Issue.2 , pp. 145-150
    • Siddiqi, S.F.1    Titchener-Hooker, N.J.2    Shamlou, P.A.3
  • 41
    • 0022000013 scopus 로고
    • The ompA signal peptide directed secretion of staphylococcal nuclease a by Escherichia coli
    • Takahara M, Hibler DW, Barr PJ, Gerlt JA, Inouye M. 1985. The ompA signal peptide directed secretion of Staphylococcal nuclease A by Escherichia coli. J Biol Chem 260:2670-2674. (Pubitemid 15139319)
    • (1985) Journal of Biological Chemistry , vol.260 , Issue.5 , pp. 2670-2674
    • Takahara, M.1    Hibler, D.W.2    Barr, P.J.3
  • 42
    • 0028430644 scopus 로고
    • Understanding flux decline in crossflow microfiltration:Part II-Effects of process parameters
    • Tarleton ES, Wakeman RJ. 1994. Understanding flux decline in crossflow microfiltration:Part II-Effects of process parameters. Chem Eng Res Des 72:431-440.
    • (1994) Chem Eng Res des , vol.72 , pp. 431-440
    • Tarleton, E.S.1    Wakeman, R.J.2
  • 43
    • 34247259031 scopus 로고    scopus 로고
    • A framework for the prediction of scale-up when using compressible chromatographic packings
    • DOI 10.1021/bp060303i
    • Tran R, Joseph JR, Sinclair A, Bracewell DG, Zhou Y, Titchener-Hooker NJ. 2007. A framework for the prediction of scale-up when using compressible chromatographic packings. Biotechnol Prog 23:413-422. (Pubitemid 46626316)
    • (2007) Biotechnology Progress , vol.23 , Issue.2 , pp. 413-422
    • Tran, R.1    Joseph, J.R.2    Sinclair, A.3    Bracewell, D.4    Zhou, Y.5    Titchener-Hooker, N.J.6
  • 45
    • 38949182338 scopus 로고    scopus 로고
    • Constructing Modified Protein-producing Escherichia coli Capable of Autohydrolysing Host Nucleic Acid during Cell Lysis
    • DOI 10.1016/S1872-2075(08)60005-9, PII S1872207508600059
    • Zhang J, Fang H, Dai H, Xie D, Chen H. 2008. Constructing modified protein-producing Escherichia coli capable of autohydrolysing host nucleic acid during cell lysis. Chinese J Biotech 24:46-52. (Pubitemid 351215158)
    • (2008) Chinese Journal of Biotechnology , vol.24 , Issue.1 , pp. 46-52
    • Zhang, J.1    Fang, H.2    Dai, H.3    Xie, D.4    Chen, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.