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Licensed Unlicensed Requires Authentication Published by De Gruyter July 6, 2019

Human Immunoglobulin G Adsorption in Epoxy Chitosan/Alginate Adsorbents: Evaluation of Isotherms by Artificial Neural Networks

Ana Carolina Moreno Pássaro, Tainá Maia Mozetic, Jones Erni Schmitz ORCID logo, Ivanildo José da Silva, Tiago Dias Martins ORCID logo and Igor Tadeu Lazzarotto Bresolin ORCID logo

Abstract

This work aimed to evaluate the interaction of human IgG in non-conventional adsorbents based on chitosan and alginate in the absence and presence of Reactive Green, Reactive Blue and Cibacron Blue immobilized as ligands. The adsorption was evaluated at 277, 288, 298 and 310 K using sodium phosphate buffer, pH 7.6, at 25 mmol L−1. The highest adsorption capacity was observed in the experiments performed with no immobilized dye, although all showed adsorption capacity higher than 120 mg g−1. Data modeling was done using Langmuir, Langmuir-Freundlich and Temkin classical nonlinear models, and artificial neural networks (ANN) for comparison. According to the parameters obtained, a possible adsorption in multilayers was observed due to protein-adsorbent and protein-protein interactions, concluding that IgG adsorption process is favorable and spontaneous. Using an ANN structure with 3 hidden neurons (single hidden layer), the MSE (RMSE) for training, test and validation were 13.698 (3.701), 11.206 (3.347) and 7.632 (2.763), respectively, achieving correlation coefficients of 0.999 in all steps. ANN modeling proved to be effective in predicting the adsorption isotherms in addition to overcoming the difficulties caused by experimental errors and/or arising from adsorption phenomenology.

Acknowledgements

The authors acknowledge the financial support from Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP, Brazil) by means of Grants 2014/23893-3 (ITL Bresolin) and 2016/18005-7 (ACM Pássaro), Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq, Brazil) by means of Grants 476726/2011-5 (ITL Bresolin) and 479942/2013-7 (IJ da Silva Jr) and Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES, Brazil) by Finance Code 001.

  1. Conflict of interest: The authors declare no financial or commercial conflict of interest.

References

[1] Abbas AK, Lichtman AH, Pillai S. Cellular and molecular immunology, 9th ed. Oxford: Elsevier LTD, 2017:544.Search in Google Scholar

[2] Ayyar BV, Arora S, Murphy C, O’kennedy R. Affinity chromatography as a tool for antibody purification. Methods. 2012;56:116–29. DOI: 10.1016/j.ymeth.2011.10.007.Search in Google Scholar PubMed

[3] Kalorama Reports. What’s trending in monoclonal antibodies (market by structure [chimeric, humanized], by target [EGFR, TNF, HER2, CD20, PD-1, other] and by disease [autoimmune, oncology, neurological, other]). 2018. Available at: https://goo.gl/iARp5D. Accessed: 26 Apr 2019.Search in Google Scholar

[4] Ecker DM, Jones SD, Levine HL. The therapeutic monoclonal antibody market. mAbs. 2015;7:9–14. DOI: 10.4161/19420862.2015.989042.Search in Google Scholar PubMed

[5] Cohn EJ, Strong L, Hughes JW, Mulford D, Ashworth J, Melin M, et al. Preparation and properties of serum and plasma protein. IV. A system for the separation into fractions of protein and lipoprotein components of biological tissues and fluids. J Am Chem Soc. 1946;68:459–75. DOI: 10.1021/ja01207a034.Search in Google Scholar

[6] Burnouf T. Modern plasma fractionation. Transfus Med Rev. 2007;21:101–17. DOI: 10.1016/j.tmrv.2006.11.001.Search in Google Scholar PubMed

[7] Burnouf T, Radosevich M. Affinity chromatography in the industrial purification of plasma proteins for therapeutic use. J Biochem Biophys Methods. 2001;49:575–86. DOI: 10.1016/S0165-022X(01)00221-4.Search in Google Scholar PubMed

[8] Perret G, Santambien P, Boschetti E. The quest for affinity chromatography ligands: are the molecular libraries the right source? J Sep Sci. 2015;38:2559–72. DOI: 10.1002/jssc.201500285.Search in Google Scholar PubMed

[9] Ritchie C. Protein purification. Mater Methods. 2012;2:134. DOI: 10.13070/mm.en.2.134.Search in Google Scholar

[10] Bayramoğlu G, Oktem HÁ, Arica MY. A dye–ligand immobilized poly(2-hydroxyethylmethacrylate) membrane used for adsorption and isolation of immunoglobulin G. Biochem Eng J. 2007;34:147–55. DOI: 10.1016/j.bej.2006.11.025.Search in Google Scholar

[11] Yemendzhiev H, Alexieva Z, Krastanov A. Decolorization of synthetic dye reactive blue 4 by mycelial culture of white-rot fungi trametes versicolor 1. Biotechnol Biotechnol Equip. 2009;23:1337–9. DOI: 10.1080/13102818.2009.10817665.Search in Google Scholar

[12] Gondim DR, Lima LP, Dias NA, de Souza MC, Bresolin IT, Adriano WS, et al. Dye ligand epoxide chitosan/alginate: a potential new stationary phase for human IgG purification. Adsorpt Sci Technol. 2012;30:701–12. DOI: 10.1260/0263-6174.30.8-9.701.Search in Google Scholar

[13] Xu C, He D, Zeng L, Luo S. A study of adsorption behavior of human serum albumin and ovalbumin on hydroxyapatite/chitosan composite. Colloids Surf B. 2009;73:360–4. DOI: 10.1016/j.colsurfb.2009.06.001.Search in Google Scholar

[14] Gondim DR, Dias NA, Bresolin ITL, Baptistiolli AM, Azevedo DC, Silva JI. Human IgG adsorption using dye-ligand epoxy chitosan/alginate as adsorbent: influence of buffer system. Adsorption. 2014;20:925–34. DOI: 10.1007/s10450-014-9636-6.Search in Google Scholar

[15] Bracco LF, Levin GJ, del Cañizo AA, Wolman FJ, Miranda MV, Cascone O. Simultaneous purification and immobilization of soybean hull peroxidase with a dye attached to chitosan mini-spheres. Biocatal Biotransform. 2017;35:306–14. DOI: 10.1080/10242422.2017.1334767.Search in Google Scholar

[16] Murphy C, Devine T, O’Kennedy R. Technology advancements in antibody purification. Antibody Technol J. 2016;6:17–32. DOI: 10.2147/ANTI.S64762.Search in Google Scholar

[17] Denizli A, Piskin EJ. Dye-ligand affinity systems. J Biochem Biophys Methods. 2001;49:391–416. DOI: 10.1016/S0165-022X(01)00209-3.Search in Google Scholar PubMed

[18] Feng Z, Shao Z, Yao J, Huang Y, Chen X. Protein adsorption and separation with chitosan-based amphoteric membranes. Polymer. 2009;50:1257–63. DOI: 10.1016/j.polymer.2008.12.046.Search in Google Scholar

[19] Kamari A, Wan Ngah WS, Liew LK. Chitosan and chemically modified chitosan beads for acid dyes sorption. J Environ Sci. 2009;21:296–302. DOI: 10.1016/S1001-0742(08)62267-6.Search in Google Scholar

[20] Schmitz JE, Bresolin IT. Prediction of the isotherms of human IgG adsorption on Ni(II)-IDA-PEVA membrane using artificial neural networks. Adsorption. 2014;20:959–65. DOI: 10.1007/s10450-014-9641-9.Search in Google Scholar

[21] Fagundes-Klen MR, Ferri P, Martins TD, Tavares CR, Silva EA. Equilibrium study of the binary mixture of cadmium–zinc ions biosorption by the Sargassum filipendula species using adsorption isotherms models and neural network. Biochem Eng J. 2007;34:136–46. DOI: 10.1016/j.bej.2006.11.023.Search in Google Scholar

[22] Xu C, Rangaiah GP, Zhao XS. Application of artificial neural network and genetic programming in modeling and optimization of ultraviolet water disinfection reactors. Chem Eng Commun. 2015;202:1415–24. DOI: 10.1080/00986445.2014.952813.Search in Google Scholar

[23] Da Silva BG, Fileti AM, Taranto OP. Drying of brazilian pepper-tree fruits (Schinus terebinthifolius Raddi): development of classical models and artificial neural network approach. Chem Eng Commun. 2015;202:1087–97. DOI: 10.1080/00986445.2014.901220.Search in Google Scholar

[24] Seolatto AA, Martins TD, Bergamasco R, Tavares CR, Cossich ES, Silva EA. Biosorption study of Ni2+ and Cr3+ by Sargassum filipendula: kinetics and equilibrium. Braz J Chem Eng. 2014;31:211–27. DOI: 10.1590/S0104-66322014000100020.Search in Google Scholar

[25] Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976;72:248–54. DOI: 10.1016/0003-2697(76)90527-3.Search in Google Scholar PubMed

[26] Vijayalakshmim MA. Pseudobiospecific ligand affinity chromatography. Trends Biotechnol. 1989;7:71–6. DOI: 10.1016/0167-7799(89)90067-X.Search in Google Scholar

[27] Johnson RD, Wang Z-G, Arnold FH. Surface site heterogeneity and lateral interactions in multipoint protein adsorption. J Phys Chem. 1996;100:5134–9. DOI: 10.1021/jp9523682.Search in Google Scholar

[28] Haupt K, Bueno SM, Vijayalakshmi MA. Interaction of human immunoglobulin G with L-histidine immobilized onto poly(ethylene vinyl alcohol) hollow-fiber membranes. J Chromatogr B. 1995;674:13–21. DOI: 10.1016/0378-4347(95)00282-9.Search in Google Scholar

[29] Franco LF, de Oliveira CL, Pessoa Filho PA. Thermodynamics of protein aqueous solutions: from the structure factor to the osmotic pressure. AIChE J. 2015;61:2871–80. DOI: 10.1002/aic.14802.Search in Google Scholar

[30] Dotto GL, Vieira ML, Gonçalves JO, Pinto LA. Removal of acid Blue 9, food Yellow 3 and FD&C Yellow n° 5 dyes from aqueous solutions using activated carbon, activated earth, diatomaceous earth, chitin and chitosan: equilibrium studies and thermodynamic. Quim Nova. 2011;34:1193–9. DOI: 10.1590/S0100-40422011000700017.Search in Google Scholar

[31] Crini G, Badot PM. Application of chitosan, a natural aminopolysaccharide, for dye removal from aqueous solutions by adsorption processes using batch studies: A review of recent literature. Prog Polym Sci. 2008;33:399–447. DOI: 10.1016/j.progpolymsci.2007.11.001.Search in Google Scholar

[32] Sharma S, Agarwal GP. Interactions of proteins with immobilized metal ions: A comparative analysis using various isotherm models. Anal Biochem. 2001;288:126–40. DOI: 10.1006/abio.2000.4894.Search in Google Scholar PubMed

[33] Kumar S, Dalvi DB, Moorthy M, Korde SS, Fondekar KP, Sahasrabudhe SD, et al. Discriminatory protein binding by a library of 96 new affinity resins: A novel dye-affinity chromatography tool-kit. J Chrom B. 2009;877:3610–8. DOI: 10.1016/j.jchromb.2009.08.045.Search in Google Scholar

[34] Johnson RD, Arnold FH. Multipoint binding and heterogeneity in immobilized metal affinity chromatography. Biotechnol Bioeng. 1995;48:437–43. DOI: 10.1002/bit.260480505.Search in Google Scholar PubMed

[35] Bresolin ITL, Ribeiro MB, Tamashiro WM, Augusto EF, Vijayalakshmi MA, Bueno SM. Evaluation of immobilized metal-ion affinity chromatography (IMAC) as a technique for IgG1 monoclonal antibodies purification: the effect of chelating ligand and support. Appl Biochem Biotechnol. 2009;160:2148–65. DOI: 10.1007/s12010-009-8734-5.Search in Google Scholar PubMed

[36] Morse G, Jones R, Thibault J, Tezel F. Neural network modelling of adsorption isotherms. Adsorption. 2011;17:303–9. DOI: 10.1007/s10450-010-9287-1.Search in Google Scholar

Received: 2019-05-08
Revised: 2019-06-09
Accepted: 2019-06-10
Published Online: 2019-07-06

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