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Persico M, Mikhaylin S, Doyen A, et al. Formation of peptide layers and adsorption mechanisms on a negatively charged cation-exchange membrane. J Colloid Interface Sci. 2017;508:488-499doi: 10.1016/j.jcis.2017.08.029.
Persico, M., Mikhaylin, S., Doyen, A., Firdaous, L., Hammami, R., Chevalier, M., Flahaut, C., Dhulster, P., & Bazinet, L. (2017). Formation of peptide layers and adsorption mechanisms on a negatively charged cation-exchange membrane. Journal of colloid and interface science, 508488-499. https://doi.org/10.1016/j.jcis.2017.08.029
Persico, Mathieu, et al. "Formation of peptide layers and adsorption mechanisms on a negatively charged cation-exchange membrane." Journal of colloid and interface science vol. 508 (2017): 488-499. doi: https://doi.org/10.1016/j.jcis.2017.08.029
Persico M, Mikhaylin S, Doyen A, Firdaous L, Hammami R, Chevalier M, Flahaut C, Dhulster P, Bazinet L. Formation of peptide layers and adsorption mechanisms on a negatively charged cation-exchange membrane. J Colloid Interface Sci. 2017 Dec 15;508:488-499. doi: 10.1016/j.jcis.2017.08.029. Epub 2017 Aug 18. PMID: 28865343.
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J Colloid Interface Sci. 2017 Dec 15;508:488-499. doi: 10.1016/j.jcis.2017.08.029. Epub 2017 Aug 18.

Formation of peptide layers and adsorption mechanisms on a negatively charged cation-exchange membrane.

Journal of colloid and interface science

Mathieu Persico, Sergey Mikhaylin, Alain Doyen, Loubna Firdaous, Riadh Hammami, Mickaël Chevalier, Christophe Flahaut, Pascal Dhulster, Laurent Bazinet

Affiliations

  1. Institute of Nutrition and Functional Foods, Dairy Research Center (STELA) and Department of Food Sciences, Université Laval, Québec, QC, Canada; Laboratoire de Transformation Alimentaire et Procédés ElectroMembranaires (LTAPEM, Laboratory of Food Processing and ElectroMembrane Processes), Université Laval, Québec, QC, Canada.
  2. Institute of Nutrition and Functional Foods, Dairy Research Center (STELA) and Department of Food Sciences, Université Laval, Québec, QC, Canada.
  3. Agri-food and Biotechnology Research Institute "Charles Violette", ProBioGEM Laboratory, Université de Lille, INRA, Lille, France.
  4. Institute of Nutrition and Functional Foods, Dairy Research Center (STELA) and Department of Food Sciences, Université Laval, Québec, QC, Canada; Laboratoire de Transformation Alimentaire et Procédés ElectroMembranaires (LTAPEM, Laboratory of Food Processing and ElectroMembrane Processes), Université Laval, Québec, QC, Canada. Electronic address: [email protected].

PMID: 28865343 DOI: 10.1016/j.jcis.2017.08.029

Abstract

Polypeptide/solid charged surface interactions are omnipresent in the biomedical and biochemical fields. The present study aimed to understand the adsorption mechanisms of a cation-exchange membrane (CEM) by a well-characterized peptide mixture at three different pH values. Results demonstrated that fouling was important at pH 6, twice lower at pH 2 and negligible at pH 10. At pH 6, ALPMHIR and TKIPAVFK sequences firstly established electrostatic interactions with the negative CEM charges (SO

Copyright © 2017 Elsevier Inc. All rights reserved.

Keywords: Cation-exchange membrane; Electrostatic and hydrophobic interactions; Peptide sequence; Peptide/peptide and peptide/membrane interactions; β-Lactoglobulin

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