Anton P J Middelberg

Summary

Affiliation: University of Cambridge
Country: UK

Publications

  1. ncbi request reprint Relation between cell disruption conditions, cell debris particle size, and inclusion body release
    Pim Van Hee
    Department of Biotechnology, Delft University of Technology, Julianalaan 67, 2628 BC Delft, The Netherlands
    Biotechnol Bioeng 88:100-10. 2004
  2. pmc Peptide interfacial adsorption is kinetically limited by the thermodynamic stability of self association
    A P Middelberg
    Department of Chemical Engineering, University of Cambridge, Pembroke Street, Cambridge CB2 3RA, United Kingdom
    Proc Natl Acad Sci U S A 97:5054-9. 2000
  3. ncbi request reprint Preparative protein refolding
    Anton P J Middelberg
    Department of Chemical Engineering, University of Cambridge, Pembroke Street, Cambridge CB2 3RA, UK
    Trends Biotechnol 20:437-43. 2002
  4. ncbi request reprint A new kinetic scheme for lysozyme refolding and aggregation
    A Mark Buswell
    Department of Chemical Engineering, University of Cambridge, Pembroke Street, Cambridge CB2 3RA United Kingdom
    Biotechnol Bioeng 83:567-77. 2003
  5. ncbi request reprint Coupling of chemical extraction and expanded-bed adsorption for simplified inclusion-body processing: optimization using surface plasmon resonance
    Woo Seok Choe
    Department of Chemical Engineering, University of Cambridge, Pembroke Street, Cambridge CB2 3RA, UK
    Biotechnol Bioeng 81:221-32. 2003
  6. ncbi request reprint The influence of molecular variation on protein interactions
    Jason G S Ho
    Department of Chemical Engineering, University of Cambridge, Pembroke Street, Cambridge CB2 3RA, United Kingdom
    Biotechnol Bioeng 84:611-6. 2003
  7. ncbi request reprint Estimating the potential refolding yield of recombinant proteins expressed as inclusion bodies
    Jason G S Ho
    Department of Chemical Engineering, University of Cambridge, Cambridge, United Kingdom
    Biotechnol Bioeng 87:584-92. 2004
  8. ncbi request reprint Production of enzymatically active ketosteroid isomerase following insoluble expression in Escherichia coli
    Matthew H Hutchinson
    Department of Chemical Engineering, University of Cambridge, Pembroke Street, Cambridge CB2 3RA, United Kingdom
    Biotechnol Bioeng 95:724-33. 2006
  9. ncbi request reprint Operational regimes for a simplified one-step artificial chaperone refolding method
    Heikki Lanckriet
    Department of Chemical Engineering, University of Cambridge, UK
    Biotechnol Prog 20:1861-7. 2004
  10. doi request reprint Intrinsic fluorescence as an analytical probe of virus-like particle assembly and maturation
    Simon J Hanslip
    Department of Chemical Engineering, University of Cambridge, Pembroke Street, Cambridge CB2 3RA, UK
    Biochem Biophys Res Commun 375:351-5. 2008

Collaborators

  • Daniel B Jones
  • Susanna S J Leong
  • Nathan R Zaccai
  • Robert J Falconer
  • Giacomo Morreale
  • Jason G S Ho
  • A Mark Buswell
  • Heikki Lanckriet
  • Simon J Hanslip
  • Woo Seok Choe
  • Andrew S Malcolm
  • Howard A Chase
  • Yap P Chuan
  • Linda H L Lua
  • Daniel I Lipin
  • Sagheer A Onaizi
  • Matthew H Hutchinson
  • Marc Langenhof
  • Chew Tin Lee
  • Pim Van Hee
  • Anders Heebøll-Nielsen
  • Robert H Clemmitt
  • Lizhong He
  • Annette F Dexter
  • Leonard K Pattenden
  • Luuk A M van der Wielen
  • Eun Gyo Lee
  • Rob G J M Van Der Lans
  • Owen R T Thomas
  • Hans P Kocher
  • Paul Ramage
  • Jemma C Miller
  • Mark Ebtinger
  • Alain A Vertès

Detail Information

Publications28

  1. ncbi request reprint Relation between cell disruption conditions, cell debris particle size, and inclusion body release
    Pim Van Hee
    Department of Biotechnology, Delft University of Technology, Julianalaan 67, 2628 BC Delft, The Netherlands
    Biotechnol Bioeng 88:100-10. 2004
    ..Nevertheless, calculations show that centrifugal separation of inclusion bodies from the enzymatically treated cells gives a high inclusion body yield and purity...
  2. pmc Peptide interfacial adsorption is kinetically limited by the thermodynamic stability of self association
    A P Middelberg
    Department of Chemical Engineering, University of Cambridge, Pembroke Street, Cambridge CB2 3RA, United Kingdom
    Proc Natl Acad Sci U S A 97:5054-9. 2000
    ..This work demonstrates that the dynamics of interfacial adsorption depend on protein thermodynamic stability, and hence structure, in a quantifiable way...
  3. ncbi request reprint Preparative protein refolding
    Anton P J Middelberg
    Department of Chemical Engineering, University of Cambridge, Pembroke Street, Cambridge CB2 3RA, UK
    Trends Biotechnol 20:437-43. 2002
    ..Combined, these developments promise to facilitate the rapid and automated determination of appropriate refolding conditions and to simplify scale-up...
  4. ncbi request reprint A new kinetic scheme for lysozyme refolding and aggregation
    A Mark Buswell
    Department of Chemical Engineering, University of Cambridge, Pembroke Street, Cambridge CB2 3RA United Kingdom
    Biotechnol Bioeng 83:567-77. 2003
    ..The new kinetic scheme gave a good a priori prediction of fed-batch refolding performance...
  5. ncbi request reprint Coupling of chemical extraction and expanded-bed adsorption for simplified inclusion-body processing: optimization using surface plasmon resonance
    Woo Seok Choe
    Department of Chemical Engineering, University of Cambridge, Pembroke Street, Cambridge CB2 3RA, UK
    Biotechnol Bioeng 81:221-32. 2003
    ..This work demonstrates that it is possible to reduce the complexity and hence the cost associated with traditional processes used to prepare purified denatured protein, ready for refolding, from cytoplasmic inclusion bodies...
  6. ncbi request reprint The influence of molecular variation on protein interactions
    Jason G S Ho
    Department of Chemical Engineering, University of Cambridge, Pembroke Street, Cambridge CB2 3RA, United Kingdom
    Biotechnol Bioeng 84:611-6. 2003
    ..We also show that the magnitude of this solvation term can be estimated using readily available data...
  7. ncbi request reprint Estimating the potential refolding yield of recombinant proteins expressed as inclusion bodies
    Jason G S Ho
    Department of Chemical Engineering, University of Cambridge, Cambridge, United Kingdom
    Biotechnol Bioeng 87:584-92. 2004
    ..Such a capability could potentially "screen," in silico, those sequences suitable for expression in bacteria from those that must be expressed in more complex hosts...
  8. ncbi request reprint Production of enzymatically active ketosteroid isomerase following insoluble expression in Escherichia coli
    Matthew H Hutchinson
    Department of Chemical Engineering, University of Cambridge, Pembroke Street, Cambridge CB2 3RA, United Kingdom
    Biotechnol Bioeng 95:724-33. 2006
    ..The intensified process in this work requires minimal optimization for recovering novel his-tagged proteins, and further improves the economic advantage of E. coli as a host organism...
  9. ncbi request reprint Operational regimes for a simplified one-step artificial chaperone refolding method
    Heikki Lanckriet
    Department of Chemical Engineering, University of Cambridge, UK
    Biotechnol Prog 20:1861-7. 2004
    ..7), best suited for lower protein concentrations. An increased chaotrope concentration resulted in higher refolding yields and an enlarged operational regime...
  10. doi request reprint Intrinsic fluorescence as an analytical probe of virus-like particle assembly and maturation
    Simon J Hanslip
    Department of Chemical Engineering, University of Cambridge, Pembroke Street, Cambridge CB2 3RA, UK
    Biochem Biophys Res Commun 375:351-5. 2008
    ..Intrinsic fluorescence is a rugged methodology that could be applied to monitoring VLP assembly and maturation unit operations during HPV vaccine manufacturing...
  11. ncbi request reprint Bioprocess-centered molecular design (BMD) for the efficient production of an interfacially active peptide
    Giacomo Morreale
    Department of Chemical Engineering, University of Cambridge, Pembroke Street, CB2 3RA, UK
    Biotechnol Bioeng 87:912-23. 2004
    ..Moreover, it is shown that BMD is a powerful strategy that can be deployed to reduce bioseparation complexity...
  12. ncbi request reprint Screening protein refolding using surface plasmon resonance
    Daniel B Jones
    Department of Chemical Engineering, University of Cambridge, Cambridge, UK
    Proteomics 4:1007-13. 2004
    ..The combination of such advantages with the high-throughput automated SPR systems currently available may be a valuable approach to determine conditions suitable for protein refolding following insoluble expression in a bacterial host...
  13. ncbi request reprint Comparison of histidine-tag capture chemistries for purification following chemical extraction
    Woo Seok Choe
    Department of Chemical Engineering, University of Cambridge, UK
    J Chromatogr A 953:111-21. 2002
    ..Robust pseudo-affinity ligands such as metal chelates show potential for selective primary recovery of unfolded proteins, and could be used for further processing such as on-column refolding...
  14. ncbi request reprint Combined in-fermenter extraction and cross-flow microfiltration for improved inclusion body processing
    Chew Tin Lee
    Department of Chemical Engineering, University of Cambridge, Pembroke Street, Cambridge CB2 3RA, United Kingdom
    Biotechnol Bioeng 85:103-13. 2004
    ..In this way refolded protein can potentially be obtained, in a relatively pure state, using only two unit operations...
  15. ncbi request reprint Critical analysis of lysozyme refolding kinetics
    A Mark Buswell
    Department of Chemical Engineering, University of Cambridge, Pembroke Street, Cambridge CB2 3RA, UK
    Biotechnol Prog 18:470-5. 2002
    ..This study demonstrates that such a pathway can exist experimentally and emphasizes the need to critically assess refolding kinetic models before their use in reactor design equations...
  16. pmc The refolding of different alpha-fetoprotein variants
    Susanna S J Leong
    Centre for Biomolecular Engineering, The University of Queensland, St Lucia, Australia
    Protein Sci 15:2040-50. 2006
    ....
  17. ncbi request reprint Continuous chromatographic protein refolding
    Heikki Lanckriet
    Department of Chemical Engineering, University of Cambridge, Pembroke Street, Cambridge CB2 3RA, UK
    J Chromatogr A 1022:103-13. 2004
    ..Moreover, it was shown that high refolding yields (72%) at high protein concentration (>1 mg ml(-1)) could be obtained...
  18. pmc The likelihood of aggregation during protein renaturation can be assessed using the second virial coefficient
    Jason G S Ho
    Department of Chemical Engineering, University of Cambridge, Cambridge CB2 3RA, UK
    Protein Sci 12:708-16. 2003
    ..SVC measurements provide a useful link, for protein folding and aggregation, between empirical observation and thermodynamics...
  19. ncbi request reprint Continuous processing of fusion protein expressed as an Escherichia coli inclusion body
    Giacomo Morreale
    Department of Chemical Engineering, University of Cambridge, Pembroke Street, CB2 3RA, Cambridge, UK
    J Chromatogr B Analyt Technol Biomed Life Sci 786:237-46. 2003
    ..Preliminary experiments proved cleavage of the fusion protein. The use of chemical extraction and continuous chromatography gives a flowsheet far superior to the traditional methods for inclusion body processing...
  20. ncbi request reprint Effect of operating variables on the yield of recombinant trypsinogen for a pulse-fed dilution-refolding reactor
    A Mark Buswell
    Department of Chemical Engineering, University of Cambridge, Pembroke Street, Cambridge CB2 3RA, UK
    Biotechnol Bioeng 77:435-44. 2002
    ..This will be controlled by micromixing effects, and hence the intensity of agitation, in a complex manner requiring further characterization...
  21. ncbi request reprint Assembly of human papillomavirus type-16 virus-like particles: multifactorial study of assembly and competing aggregation
    Simon J Hanslip
    Department of Chemical Engineering, University of Cambridge, Pembroke Street, Cambridge, CB2 3RA, UK
    Biotechnol Prog 22:554-60. 2006
    ....
  22. ncbi request reprint A simplified bioprocess for human alpha-fetoprotein production from inclusion bodies
    Susanna S J Leong
    Centre for Biomolecular Engineering, Division of Chemical Engineering, The University of Queensland, St Lucia, Queensland 4072, Australia
    Biotechnol Bioeng 97:99-117. 2007
    ..This highly intensified and simplified process is expected to be of general utility for the preparation of other therapeutic candidates expressed as inclusion bodies...
  23. ncbi request reprint Efficient inclusion body processing using chemical extraction and high gradient magnetic fishing
    Anders Heebøll-Nielsen
    Center for Process Biotechnology, BioCentrum DTU, Technical University of Denmark, DK 2800, Kgs Lyngby, Denmark
    Biotechnol Prog 19:887-98. 2003
    ..Over 70% of the initial L1 present was recovered within the HGMF rig in a highly clarified form in two batch elution cycles with an overall purification factor of approximately 10...
  24. ncbi request reprint Mechanical properties of interfacial films formed by lysozyme self-assembly at the air-water interface
    Andrew S Malcolm
    Centre for Biomolecular Engineering, University of Queensland, St Lucia, QLD 4072, Australia
    Langmuir 22:8897-905. 2006
    ....
  25. ncbi request reprint Directed disassembly of an interfacial rubisco protein network
    Sagheer A Onaizi
    Centre for Biomolecular Engineering, The Australian Institute for Bioengineering and Nanotechnology, University of Queensland, St Lucia QLD 4072, Australia
    Langmuir 23:6336-41. 2007
    ....
  26. doi request reprint High-level expression of soluble viral structural protein in Escherichia coli
    Yap P Chuan
    Centre for Biomolecular Engineering, The University of Queensland, St Lucia, Brisbane 4072, Australia
    J Biotechnol 134:64-71. 2008
    ..coli rare codons; using a strategically modified host cell could provide a simpler and cheaper alternative...
  27. doi request reprint Quaternary size distribution of soluble aggregates of glutathione-S-transferase-purified viral protein as determined by asymmetrical flow field flow fractionation and dynamic light scattering
    Daniel I Lipin
    Centre for Biomolecular Engineering, Australian Institute for Bioengineering and Nanotechnology, The University of Queensland, Brisbane, Queensland 4072, Australia
    J Chromatogr A 1190:204-14. 2008
    ..The finding that GST-tagged viral proteins exist as soluble aggregates has implications for existing immunological studies that utilize them...
  28. ncbi request reprint Controlled oxidative protein refolding using an ion-exchange column
    Marc Langenhof
    Centre for Biomolecular Engineering, University of Queensland, St Lucia, QLD 4072, Australia
    J Chromatogr A 1069:195-201. 2005
    ..Moreover, it is possible to strictly control the oxidative refolding environment once denatured protein is bound to the ion-exchange column, thus allowing precisely controlled oxido-shuffling...