Purification Of Amino Acids And Small Peptides With Hollow Fibers

Abstract

Permeation through hollow fibers made of a perfluorinated ionomer membrane of the Nafion type is shown to be a possible way to separate amino acids and small peptides. The fiber has a surface area to volume ratio of 56 cm2 cm-3. Twenty-six different amino acids and small peptides with up to six amino acid units were used for permeation studies. The results show that the bulk pH is the essential parameter acting on the permeation rates and diffusion coefficients through the tubing wall. The cationic forms of the solutes, at a pH lower than their isoelectric points, were highly retained by the cation-exchange membrane. The anionic forms of the solutes, at a pH higher than the isoelectric point, were less retained. The zwitterionic and non-ionic forms had the highest permeation rates, reaching 2.2 x 10-3 s-1. The effect of methanol addition was studied. The permeation rates increased, but the selectivity decreased. © 1991.

Department(s)

Chemistry

Comments

Centre National de la Recherche Scientifique, Grant DEF602-88ER1389

Keywords and Phrases

Amino acids; Hollow fibres; Ion exchange; Nafion membrane; Peptides

International Standard Serial Number (ISSN)

0003-2670

Document Type

Article - Journal

Document Version

Citation

File Type

text

Language(s)

English

Rights

© 2023 Elsevier, All rights reserved.

Publication Date

01 Jan 1991

Link to Full Text

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