I'm currently trying to separate a protein from commercial cream (details below). I've been able to separate it using Benzethonium chloride in a BP aqueous cream but I am not getting great extraction percentages with the new cream. Any suggestions? Protein column? Different chemical?
Water (Aqua),
Glycerin,
Caprylic/Capric Triglyceride,
Glyceryl Stearate,
Honey (Mel),
Cetearyl Alcohol,
Isopropyl Myristate,
Dimethicone,
PEG-100
Stearate,
Ceteareth-20,
Phenoxyethanol,
Caprylyl Glycol,
Sorbitan Stearate,
Carbomer,
Disodium EDTA,
Diazolidinyl Urea,
Sodium Metabisulfite,
Sodium Hydroxide.
Is this for an analytical (qualitative or quantitative) application or are you trying to recover all the target material from a production lot for re-processing? Is the protein a relatively short peptide or full length molecule such as structural, enzymatic, signalling, defensive, or nutritional proteins? For example, if it's an analytical goal then there are two-step specific MALDI methods for small peptides that are qualitative and maybe semi-quantitative that do not require sample processing for cosmetic formulations. I assume this is the British Pharmacopeia formulation for a skin cosmetics? You may need another solvent such as DMSO but what is the molecule's pI, size, and does it have to have native structure after extraction/recovery?
Guessing at what your situation/conditions might be, this may help: https://www.dropbox.com/s/5ad7pjyqayvmmhw/Kafka_et_al-2010-Biomedical_Chromatography.pdf?dl=1 Something similar was done in previous experience with methionyl bovine somatotropin with cream formulations.
You might be relying on the binding with a quat. amine to pull out your solute into an aqueous environment but the detergents, pH, and other vehicle components may interfere with binding capacity. Once extracted into an aqueous solvent, the detergents may still be binding to the protein/peptide but might be removable with detergent binding resins.
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