Partitioning of whey proteins, bovine serum albumin and porcine insulin in aqueous two-phase systems.
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 alpha-lactoalbumin (alpha-La) concentrated in the upper phase and beta-lactoglobulin (beta-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.
Alves
J G
JG
Food Engineering Department, FEA, State University of Campinas, SP, Brazil.
Chumpitaz
L D
LD
da Silva
L H
LH
Franco
T T
TT
Meirelles
A J
AJ
D000818:Animals; D002417:Cattle; D002951:Citrates / Q000737:chemistry; D007328:Insulin / Q000302:isolation & purification*; D008894:Milk Proteins / Q000302:isolation & purification*; D011092:Polyethylene Glycols / Q000737:chemistry; D012710:Serum Albumin, Bovine / Q000302:isolation & purification*; D000077559:Sodium Citrate; D013552:Swine; D000067816:Whey Proteins
D002951:Citrates; D007328:Insulin; D008894:Milk Proteins; D000067816:Whey Proteins; D000077559:Sodium Citrate; D012710:Serum Albumin, Bovine; D011092:Polyethylene Glycols