Examination of the Effects of Activated Carbon Produced from Coal Using Single-Step H3PO4/N2+H2O Vapor Activation on the Adsorption of Bovine Serum Albumin at Different Temperatures and pH Values
Abstract
This study examined protein adsorption equilibrium and kinetics on activated carbon (AC) that we obtained from coal by single-step H3PO4 activation under N2+H2O vapor at 800 °C. Surface properties, pore size distribution, and volumes of AC were determined using volumetric method with N2 adsorption at 77 K. Also, the textural properties were characterized by SEM-EDAX and XRD. The zeta potential values were measured to elucidate the electrostatic interactions between the protein and AC. The obtained AC discrete system was also used as an adsorbent for adsorbing bovine serum albumin (BSA) from aqueous solution. The effects of pH (4.0, 5.0, and 7.4) and temperatures (20, 30 and 40 °C) on the adsorption of BSA on AC were examined. The surface area, micropore, mesopore and total pore volumes of AC were found to be 1175 m2/g, 0.477 cm3/g, 0.061 cm3/g and 0.538 cm3/g, respectively. The optimum temperature for AC in BSA adsorption was found to be 40 °C and the pH was found to be 4.0. The highest BSA adsorption was found to be 159 mg/g and pH to be 4.0. The experimental equilibrium data were compared with the Langmuir and Freundlich models and found to be compatible with both models. The adsorption process is best described by the pseudo-first-order kinetic model. As a result, it was found out that AC obtained by single step H3PO4/N2+H2O vapor activation is an effective adsorbent for the adsorption of BSA from aqueous solution.
Keywords
References
- 1. Lu JR, Zhao X, Yaseen M. Protein adsorption studied by neutron reflection. Current Opinion in Colloid & Interface Science. 2007;12(1):9-16.
- 2. Hinderliter A, Almeida PF, Creutz CE, Biltonen RL. Domain formation in a fluid mixed lipid bilayer modulated through binding of the C2 protein motif. Biochemistry. 2001;40(13):4181-91.
- 3. Rabe M, Verdes D, Seeger S. Understanding protein adsorption phenomena at solid surfaces. Advances in colloid and interface science. 2011;162(1):87-106.
- 4. Kalasin S, Santore MM. Non-specific adhesion on biomaterial surfaces driven by small amounts of protein adsorption. Colloids and Surfaces B: Biointerfaces. 2009;73(2):229-36.
- 5. Liu J, Lee ML. Permanent surface modification of polymeric capillary electrophoresis microchips for protein and peptide analysis. Electrophoresis. 2006;27(18):3533-46.
- 6. Roach P, Eglin D, Rohde K, Perry CC. Modern biomaterials: a review—bulk properties and implications of surface modifications. Journal of Materials Science: Materials in Medicine. 2007;18(7):1263-77.
- 7. Chen H, Yuan L, Song W, Wu Z, Li D. Biocompatible polymer materials: role of protein–surface interactions. Progress in Polymer Science. 2008;33(11):1059-87.
- 8. Cole MA, Voelcker NH, Thissen H, Griesser HJ. Stimuli-responsive interfaces and systems for the control of protein–surface and cell–surface interactions. Biomaterials. 2009;30(9):1827-50.
Details
Primary Language
English
Subjects
Engineering, Chemical Engineering
Journal Section
Research Article
Publication Date
September 1, 2017
Submission Date
October 2, 2017
Acceptance Date
December 22, 2017
Published in Issue
Year 2018 Volume: 5 Number: 1
Cited By
Manyetik Aktif Karbon/ZnO kompozitinin Sentezlenmesi ve Boyar Madde Giderimi Üzerine Denge ve Kinetik Uygulaması
European Journal of Science and Technology
https://doi.org/10.31590/ejosat.673884
