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Iranian Biomedical Journal، جلد ۲۶، شماره ۱، صفحات ۸۵-۹۰
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عنوان انگلیسی A Simplified Process for Purification and Refolding of Recombinant Human Interferon-α2b
چکیده انگلیسی مقاله Background: Interferon α-2b is a vital biotherapeutic produced through the recombinant DNA technology in E. coli. The recombinant IFN-α2b normally appears as intercellular IBs, which requires intensive refolding and purification steps. Method: Purification of IFN-α2b from solubilized IB was performed using two-phase extraction. To optimize refolding conditions, the effects of pH and different additives, including cysteine, cystine, urea, glycerol, Triton X-100, NaCl, and arginine, were investigated. Optimal refolding buffer (0.64 mM of urea, 5.57 mM of cysteine ​​, and 1.8 mM of cystine) was obtained using RSM. The refolding process was performed by an optimized refolding buffer in the dilution and fed-batch refolding method at different protein concentrations (25-1000 µg/mL). Result:  At a final protein concentration of 500 µg/mL, the fed-batch refolding method yielded in a biological activity of 2.24 × 108 IU/mg, which was nearly twice that of dilution method. Conclusion: Fed-batch refolding method resulted in the biologically active IFN-α2b with high purity, which can be used for research and industrial purposes.
کلیدواژه‌های انگلیسی مقاله Interferon alpha-2b, Inclusion bodies, Protein refolding
نویسندگان مقاله | Nima Hezarjaribi
Department of biology, Faculty of basic science, Islamic Azad University Science and Research Branch, Tehran, Iran


| Mohammad Reza Fazeli
Department of Drug & Food Control, Pharmaceutical Quality Assurance Research Center, Faculty of Pharmacy, Tehran University of Medical science, Tehran, Iran
نشانی اینترنتی http://ibj.pasteur.ac.ir/browse.php?a_code=A-10-4555-1&slc_lang=en&sid=1
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کد مقاله (doi)
زبان مقاله منتشر شده en
موضوعات مقاله منتشر شده Pharmaceutical Biotechnology
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