Jglf. Alves et al., Partitioning of whey proteins, bovine serum albumin and porcine insulin inaqueous two-phase systems, J CHROMAT B, 743(1-2), 2000, pp. 235-239
Partitioning of the proteins from cheese whey, bovine serum albumin and por
cine insulin were analysed using aqueous two-phase systems (ATPS) prepared
with PEG-phosphate, PEG-citrate and PEG-maltodextrin (MD). Proteins were qu
antified through one of the following methods: FPLC, Bradford and spectroph
otometry at 280 nm. Results showed that whey proteins partitioned unevenly
on the phases of the systems used, with alpha-lactoalbumin (alpha-La) conce
ntrated in the upper phase and beta-lactoglobulin (beta-Lg) in the lower. A
lbumin in PEG-MD systems concentrated in the MD-rich lower phase. Porcine i
nsulin showed great affinity with the PEG-rich phase, its partition coeffic
ient was always over 10 and increases with PEG molecular mass. (C) 2000 Els
evier Science B.V. All rights reserved.