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Industrial Biotechnology Centre

Picture by IBM Research

School of Biosciences

The School of Biosciences at the University of Kent has a long history of delivering high-quality research and training across the Bioprocessing remit. This has resulted in the output of personnel trained in diverse areas of bioprocessing, high-quality research publications, and IP that is used for novel manufacturing approaches in recombinant protein bioprocessing. Central to this continued success has been the recognition that research and training in bioprocessing will provide a greater understanding of the biology underpinning advances in bioprocessing. Projects have been designed to work with funding agencies, academic colleagues and industrial partners to deliver research and training in areas of strength at Kent that help meets the current strategic need of the industrial and academic bioprocessing community.

Research expertise


Recombinant protein expression systems

Professor Mark SmalesYeast (Saccharomyces cerevisiae,
Pichia pastoris)

Professor Mick Tuite
Dr Peter Nicholls
Escherichia coli
Professor Martin Warren
Dr Tobias von der Haar
Dr Richard Williamson
Dr Peter Klappa

Microbial Cell Engineering

Professor Mick Tuite
Professor Martin Warren
Dr Tobias von der Haar
Dr Dan Mulverhill

Animal Cell Engineering

Professor Mark Smales Dr Martin Carden

Synthetic Biology and Metabolic Engineering

Professor Martin Warren Professor Mark Smales

Systems Biology

Dr Tobias von der Haar

Molecular Processing Science

Professor William Gullick
Professor Mark Smales
Professor Mick Tuite
Professor Martin Warren
Dr Anthony Baines
Dr Mark Howard
Dr Peter Klappa
Dr Dan Lloyd
Dr Peter Nicholls
Dr Richard Williamson
Dr Gary Robinson
Dr Marcus Allen
Dr Martin Carden
Dr Tobias von der Haar
Dr Dan Mulvihill
Dr Campbell Gourlay

Technologies available for licensing

Improved protein secretion
~ Professor Mick Tuite


Hayes NVL, Smales CM, Klappa P. Protein disulfide isomerise does not control recombinant IgG4 productivity in mammalian cell lines. Biotechnology and Bioengineering, in press.

Josse L, Smales CM, Tuite MF (2010) Transient expression of human TorsinA enhances secretion of two functionally distinct proteins in cultured Chinese hamster ovary (CHO) cells. Biotechnology and Bioengineering105 556-566.

Masterton RJ, Roobol A, Al-Fageeh MB, Carden MJ, Smales CM (2010) Post-translational events of a model reporter protein proceed with higher fidelity and accuracy upon mild hypothermic culturing of Chinese hamster ovary cells. Biotechnology and Bioengineering105 215-220.

Povey JF, Perez-Moral N, Noel TR, Parker R, Howard MJ, Smales CM (2009) Investigating variables and mechanisms that influence protein integrity in low water content amorphous carbohydrate matrices. Biotechnology Progress25 1217-1227.

Al-Fageeh, M.B. & Smales, C.M. (2009) Cold-inducible RNA binding protein (CIRP) expression is modulated by alternative mRNAs.  RNA, 15, 1164-1176.

Cottier, F. & Mühlschlegel, F.A. (2009) Sensing the environment: Response of Candida albicans to the X factor.  FEMS Microbiology Letters, 295, 1-9.

Leadsham, J.E., Miller, K., Ayscough, K.R. Colombo, S., Martegani, E., Sudbery, P. & Gourlay, C.W. (2009) Whi2p links nutritional sensing to actin-dependent Ras-cAMP-PKA regulation and apoptosis in yeast.  Journal of Cell Science, 122, 706-715.

Mead, E.J., Chiverton, L.M., Smales, C.M. & von der Haar, T. (2009) Identification of the limitations on recombinant gene expression in CHO cell lines with varying luciferase production rates.  Biotechnology and Bioengineering, 102, 1593-1602.

Brindley, A.A., Pickersgill, R.W., Partridge, J.C., Dunstan, D.J., Hunt, D.M. & Warren, M.J. (2008) Enzyme sequence and its relationship to hyperbaric stability of artificial and natural fish lactate dehydrogenases.  PLoS ONE, 3, e2042.

Nguyen, V.D., Wallis, K., Howard, M.J., Haapalainen, A.M., Salo, K.E.H., Saaranen, M.J., Sidhu, A., Wierenga, R.K., Freedman, R.B., Ruddock, L.W. & Williamson, R.A. (2008) Alternative conformations of the x region of human protein disulphide-isomrase modulate exposure of the substrate binding b’ domain.  Journal of Molecular Biology, 383, 1144-1155.

Parsons, J.P., Dinesh, S.D., Deery, E., Leech, H.K., Brindley, A.A., Heldt, D., Frank, S., Smales, C.M., Lunsdorf, H., Rambach, A., Gass, M.H., Bleloch, A., McClean, K.J., Munro, A.W., Rigby, S.E., Warren, M.J. & Prentice, M.B. (2008) Biochemical and structural insights into bacterial organelle form and biogenesis.   Journal of Biological Chemistry, 283, 14366-14375.

Byrne, L.J., Box, B.S., Cole, D.J., Ridout, M.S., Morgan, B.J.T. & Tuite, M.F. (2007) Cell division is essential for elimination of the yeast [PSI+] prion by guanidine hydrochloride.  Proceedings of the National Academy of Sciences of the United States of America, 104, 11688-11693.

Karala, A.-R., Psarrakos, P., Ruddock, L.W. & Klappa, P. (2007) Protein disulfide isomerases from C. elegans are equally efficient at thiol-disulfide exchange in simple peptide-based systems but show differences in reactivity towards protein substrates.  Antioxidants and Redox Signaling, 9, 1815-1823.

von der Haar, T., Oku, Y., Ptushkina, M., Moerke, N., Wagner, G., Gross, J.D. and McCarthy, J.E.G. (2006) Folding transitions during assembly of the eukaryotic mRNA cap-binding complexJ. Mol. Biol. 356, 982-992.

Scientific objectives and themes

Molecular Processing research and training at Kent is initially focussed upon our strengths, investigating the mechanisms and cellular requirements that influence disease states and the synthesis of therapeutic agents and biomedicines from biological systems (e.g. bacterial, yeast, mammalian systems). The initial scientific objectives and themes of work in the Centre from Biosciences are: