Process Development for the Production and Purification of PEGylated RhG-CSF Expressed in Escherichia coli.

Background And Objectives: Recombinant human granulocyte-colony stimulating factor (rhG-CSF) and its PEGylated form (PEG-GCSF) are used in cancer therapy. Thus, developing a more cost-effectively method for expressing rhG-CSF and the PEGylation optimization of rhG-CSF by reaction engineering and subsequent purification strategy is necessary.

Methods: RhG-CSF expression in Escherichia coli BL21 (DE3) was carried out by auto-induction batch fermentation and improved for maximizing rhG-CSF productivity.

Continuous biodegradation of parathion by immobilized Sphingomonas sp. in magnetically fixed-bed bioreactors and evaluation of the enzyme stability of immobilized bacteria.

Magnetically-modified Sphingomonas sp. was prepared using covalent binding of magnetic nanoparticles on to the cell surface. The magnetic modified bacteria were immobilized in the fixed-bed bioreactors (FBR) by internal and external magnetic fields for the biodetoxification of a model organophosphate, parathion: 93 % of substrate (50 mg parathion/l) was hydrolyzed at 0.

Immobilization of magnetic modified Flavobacterium ATCC 27551 using magnetic field and evaluation of the enzyme stability of immobilized bacteria.

The magnetic modified Flavobacterium sp. was prepared by covalently binding carboxylate-modified magnetic nanoparticles, and also, ionic adsorption of magnetic Fe(3)O(4) nanoparticles on the cell surface. The magnetic modified bacteria were immobilized by both internal and external magnetic fields.