These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Single and two-component cation-exchange adsorption of the two pure major whey proteins.
    Author: El-Sayed MM, Chase HA.
    Journal: J Chromatogr A; 2009 Dec 11; 1216(50):8705-11. PubMed ID: 19298967.
    Abstract:
    Adsorption of pure alpha-lactalbumin (ALA) and beta-lactoglobulin (BLG) to the cation exchanger SP Sepharose FF was studied at pH 3.7 with the purpose of developing a process for isolating them from whey. Measurement of Langmuir parameters describing adsorption equilibrium in batch experiments and protein breakthrough time values in 1-ml packed-beds at a linear velocity of 158 cm/h and initial concentrations of 3 mg/ml for BLG and 1.5 mg/ml for ALA suggested the feasibility of using this adsorbent to separate the two proteins when present in a mixture. Subsequent experiments with 5-ml columns at the above concentrations and a linear velocity of 30 cm/h confirmed this and showed evidence of competitive adsorption as ALA displaced and eluted all BLG from the column in a pure form, and the remaining ALA could be eluted thereafter at high purity and with 91% recovery.
    [Abstract] [Full Text] [Related] [New Search]