Dr Jingxiu Bi

Senior Lecturer

B.E. (China), M.E. (CAS, China), PhD (CAS, China)

Location: Room N212 Engineering North
Email: jingxiu.bi@adelaide.edu.au
Phone: + 61 8 8303 4118
FAX: +61 8 8303 4373

Research Interests

• High producing mammalian cell lines development by gene regulation and scale up culture; 
• Bioprocess design and development of proteins purification for biopharmaceutical products; 
• Investigation of assembly characterization of virus like particles in the purification process routes

Publications

Book Chapter  

• Zeng A.-P., and Bi J-X., Chapter 9: Cell Culture Kinetics And Modeling. (2005). In: Cell Culture Technology for Pharmaceutical and Cellular Therapies. Eds S. S. Ozturk and W.-S. Hu . Marcel Dekker Inc. New York, p299-348;

Journal Publication  

• Bi J.-X., Wirth M., Beer C., Zeng A.-P. (2002). Dynamic Characterization Of Recombinant Chinese Hamster Ovary Cells Containing An Inducible c-fos Promoter GFP Expression System As A Biomarker, J. of Biotechnology, 93, 231-241;
• Bi J-X., Buhr P., Zeng A.-P., Wirth M., (2003), Human c-fos Promoter Mediates High-Level Inducible Expression In Various Mammalian Cell Lines, Biotechnology and Bioengineering. 81, 847-854;
• Ibarra N., Watanabe S., Bi J-X., Shuttleworth J., Al-Rubeai M. (2003). Modulation Of Cell Cycle For Enhancement Of Antibody Productivity In Perfusion Culture Of NS0 Cells. Biotechnology Proggress, 19, 224-228;
• Bi J.-X, Shuttleworth J, Al-Rubeai M. (2004). Uncoupling Of Cell Growth And Proliferation Results In Enhancement Of Productivity In P21cip1-Arrested CHO Cells. Biotechnology and Bioengineering; 85, (7):741-749;
• Yun Q., He M.L., Xing W.C, Bi J.X., Ma G.H. and Su Z.G. (2004). A novel tetrafunctional reagent for simultaneous intramolecular and intermolecular cross-linking of bovine hemoglobin. Biotechnology Letter, 26, 1359-1363;
• Zhi W.B., Song J.N., Ouyang F. and Bi J.X., (2005) Application Of Response Surface Methodology To The Modeling Of a-Amylase Purification By Aqueous Two-Phase Systems. Journal of Biotechnology, 118, 157-165;
• Zhou W.B., Bi J.X., Janson J.C., Su Z.G., (2005). Ion Exchange Chromatography of Hepatitis B Virus Surface Antigen from Recombinant Chinese Hamster Ovary (CHO) Cell Line. Journal of Chromatography A, 1095, 119-125;
• Zhi W, Song J, Bi J.X, Ouyang F. (2005) Partial purification of α-amylase from culture supernatant of Bacillus subtilis in aqueous two-phase systems. Bioprocess and Biosystems Engineering. 27, 3-8;
• Yun Q., Yang R.E., Chen T., Bi J.X., Ma G.H., Su Z.G, (2005) Reproducible preparation and effective seperation of PEGylated reccombinant human granulocyte colony-stimulaing factor with novel â??PEG-pelletâ?? PEGylation mode and ion exchange chrmomatography, Journal of Biotechnology, 118, 67-74;
• Li, X.N., Sun H.H., Zhang G.F., Bi J.X., Ma R.Y, Su Z.G., (2005) A cyanopropyl reversed phase chromatography enables resolution of huperzine A and B on analytical and preparative scales. Journal of Seperation Science 28, 2363-9;
• Zhou W.B., Bi J.X., Janson J.C., Su Z.G., (2006), Molecular Characterization of Recombinant Hepatitis B Surface Antigen from Chinese Hamster Ovary and Hansenula polymorpha Cells by High-Performance Size Exclusion Chromatography and Multi-Angle Laser Light scattering, Journal of Chromatography B. 838, 71-77;
• Huang Y.D., Bi J.X., Zhou W.B., Su Z.G., (2006) Improving recovery of recombinant hepatitis B virus surface antigen by ion exchange chromatography support with low ligand density. Process of Biochemistry, 41:2320-2326;
• Zhou F., Bi J.X. Zeng A.-P., Yuan J.Q., A macrokinetic and regulator model for myeloma cell culture based on metabolic balance of pathways. Process of Biochemistry 2006, 41:2207-2217;
• Li Y., Bi J.X., Zhou W.B., Su Z.G, (2007) Characterization of the large size aggregation of Hepatitis B virus surface antigen (HBsAg) formed in ultrafiltration process. Process of Biochemistry, 42: 315-319;
• Zhou W.B., Bi J.X., Li Y., Su Z.G., (2007), A highly efficient hydrophobic interaction chromatographic absorbent improved the purification of Hepatitis B Surface Antigen (HBsAg) derived from Hansenula polymorpha cell. Process of Biochemistry, 42:751-756;
• Huang Y.D., Bi J.X., Zhou W.B., Li Y., Su Z.G., (2007). A highly efficient integrating chromatographic procedure for the purification of recombinant hepatitis B surface antigen from Hansenula polymorpha, Protein Expression and Purification, 56:301-310;