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|Type:||Artigo de periódico|
|Title:||Partitioning Of Whey Proteins, Bovine Serum Albumin And Porcine Insulin In Aqueous Two-phase Systems|
Da Silva L.H.M.
|Abstract:||Partitioning of the proteins from cheese whey, bovine serum albumin and porcine insulin were analysed using aqueous two-phase systems (ATPS) prepared with PEG-phosphate, PEG-citrate and PEG-maltodextrin (MD). Proteins were quantified through one of the following methods: FPLC, Bradford and spectrophotometry at 280 nm. Results showed that whey proteins partitioned unevenly on the phases of the systems used, with α-lactoalbumin (α-La) concentrated in the upper phase and β-lactoglobulin (β-Lg) in the lower. Albumin in PEG-MD systems concentrated in the MD-rich lower phase. Porcine insulin showed great affinity with the PEG-rich phase, its partition coefficient was always over 10 and increases with PEG molecular mass. (C) 2000 Elsevier Science B.V.|
|Appears in Collections:||Unicamp - Artigos e Outros Documentos|
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