After ultrafiltration of a protein mixture, the fraction of proteins that is retained on the ultrafiltration membrane; Is this fraction usable and how to obtain it without affecting the native structure of proteins
Cristiano José De Andrade
Thank you. What should be the pH of the buffer. Should it correspondence to the isoelectric pH of the protein.
No, on the contrary. You should used the optimum pH (in terms of solubility).
Hello Waqas N Baba;
Good question. I understand that after the ultrafiltration process, as the retentate you have a suspension with a moderate concentration of proteins, and you want to recover such proteins. If this is correct, you need to precipitate your protein. As you suggested above, you need to adjust the pH of your retentate suspension to the isolectric point of the protein in order to obtain a precipitate. It does not make sense to use the pH to solubilize your protein as it was suggested above, since the protein is already solubilized in your suspension. After protein precipitation you can use centrifugation followed by a drying process (spray or freeze drying) to recover your protein as a powder.
For more information on protein isolation and purification from plant seeds by alkaline extraction and membrane filtration, I recommend that you read the works of Prof. L. Diosady from the University of Toronto.
https://www.researchgate.net/profile/Ll-Diosady
Here I attached the RG link to a couple of papers by Prof. Diosady on this topic:
Article Production of protein isolates from yellow mustard meals by ...
Article Production of mustard protein isolates from oriental mustard...
Hope this is useful for your research.
Regards
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