title: [Progress in purification of human serum albumin].
abstract: Human serum albumin(HSA) has been used clinically to treat a number of diseases with high dosage. Extremely pure puoduct is required in large-scale production. Plasma-derived HSA(pHSA) has long been produced by precipitation methods. Among them cold ethanol precipitation is dominant. However, chromatographic purification of HSA has been increasingly studied in the last few years. Application of chromatography, especially ionexchange, affinity, and size-exclusion, has opened a new area in the production of pHSA. A new challenge is the purification of recombinant HSA(rHSA). A successful approach involves STREAMLINE expanded bed adsorption to direct capture the target product from the fermentation broth. This novel process eliminates the need to separate the cells by centrifugation or membrane filtration. Ion exchange chromatography and hydrophobic chromatography play a central role in the purification scheme. Integration with other chromatographic techniques such as size-exclusion, metal chelate, and affinity gives improved purification results. Though innovative, the purification of rHSA still needs further improvement and optimization to increase product purity and process recovery.
authors.affiliation: National Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, PO Box 353, Beijing 100080, China.
authors.forename: Xiu-Ling
authors.initials: XL
authors.lastname: Lu
authors.forename: Zhi-Guo
authors.initials: ZG
authors.lastname: Su
mesh_terms: D006801:Humans; D011994:Recombinant Proteins / Q000302:isolation & purification; D012709:Serum Albumin / Q000302:isolation & purification*
chemical_list: D011994:Recombinant Proteins; D012709:Serum Albumin