Polyelectrolytes-protein complexes: a viable platform in the downstream processes of industrial enzymes at scaling up level

Complexation between proteins and polyelectrolytes through electrostatic interactions gives either soluble or non‐soluble complexes, leading to phase separation. The formation and the stability of these complexes are influenced by pH, ionic strength, ratio between protein and polyelectrolyte and cha...

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Published in	Journal of chemical technology and biotechnology (1986) Vol. 91; no. 12; pp. 2921 - 2928
Main Authors	Woitovich Valetti, Nadia, Brassesco, M Emilia, Picó, Guillermo Alfredo
Format	Journal Article
Language	English
Published	Chichester, UK John Wiley & Sons, Ltd 01.12.2016 Wiley Subscription Services, Inc
Subjects	bioseparation Chromium downstream processes downstream processes, bioseparation Electrostatics enzyme purification Enzymes Phase separation Polyelectrolytes Precipitation (chemistry) Proteins Scaling up
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Abstract	Complexation between proteins and polyelectrolytes through electrostatic interactions gives either soluble or non‐soluble complexes, leading to phase separation. The formation and the stability of these complexes are influenced by pH, ionic strength, ratio between protein and polyelectrolyte and charge density of protein and polyelectrolyte. This review presented the advantages on the protein precipitation by adding a polyelectrolyte solution to a natural enzyme source (microbiological, vegetal or animal homogenate), over the classical precipitation methods. An enzyme can be precipitated like non‐soluble complex, separated and then re‐dissolved, thus the method works, at the same time, like concentrative and pre‐purification steps together. © 2016 Society of Chemical Industry
AbstractList	Complexation between proteins and polyelectrolytes through electrostatic interactions gives either soluble or non-soluble complexes, leading to phase separation. The formation and the stability of these complexes are influenced by pH, ionic strength, ratio between protein and polyelectrolyte and charge density of protein and polyelectrolyte. This review presented the advantages on the protein precipitation by adding a polyelectrolyte solution to a natural enzyme source (microbiological, vegetal or animal homogenate), over the classical precipitation methods. An enzyme can be precipitated like non-soluble complex, separated and then re-dissolved, thus the method works, at the same time, like concentrative and pre-purification steps together. Complexation between proteins and polyelectrolytes through electrostatic interactions gives either soluble or non-soluble complexes, leading to phase separation. The formation and the stability of these complexes are influenced by pH, ionic strength, ratio between protein and polyelectrolyte and charge density of protein and polyelectrolyte. This review presented the advantages on the protein precipitation by adding a polyelectrolyte solution to a natural enzyme source (microbiological, vegetal or animal homogenate), over the classical precipitation methods. An enzyme can be precipitated like non-soluble complex, separated and then re-dissolved, thus the method works, at the same time, like concentrative and pre-purification steps together. © 2016 Society of Chemical Industry Abstract Complexation between proteins and polyelectrolytes through electrostatic interactions gives either soluble or non‐soluble complexes, leading to phase separation. The formation and the stability of these complexes are influenced by pH, ionic strength, ratio between protein and polyelectrolyte and charge density of protein and polyelectrolyte. This review presented the advantages on the protein precipitation by adding a polyelectrolyte solution to a natural enzyme source (microbiological, vegetal or animal homogenate), over the classical precipitation methods. An enzyme can be precipitated like non‐soluble complex, separated and then re‐dissolved, thus the method works, at the same time, like concentrative and pre‐purification steps together. © 2016 Society of Chemical Industry
Author	Brassesco, M Emilia Woitovich Valetti, Nadia Picó, Guillermo Alfredo
Author_xml	– sequence: 1 givenname: Nadia surname: Woitovich Valetti fullname: Woitovich Valetti, Nadia organization: Institute of Biotechnological and Chemical Processes (IPROBYQ - CONICET) and Technology Department, Faculty of Biochemical and Pharmaceutical Sciences, National University of Rosario, Suipacha 570, S2002RLK, Rosario, Argentina – sequence: 2 givenname: M Emilia surname: Brassesco fullname: Brassesco, M Emilia organization: Institute of Biotechnological and Chemical Processes (IPROBYQ - CONICET) and Technology Department, Faculty of Biochemical and Pharmaceutical Sciences, National University of Rosario, Suipacha 570, S2002RLK, Rosario, Argentina – sequence: 3 givenname: Guillermo Alfredo surname: Picó fullname: Picó, Guillermo Alfredo email: gpico@fbioyf.unr.edu.ar, pico@iprobyq-conicet.gov.ar, gpico@fbioyf.unr.edu.ar organization: Institute of Biotechnological and Chemical Processes (IPROBYQ - CONICET) and Technology Department, Faculty of Biochemical and Pharmaceutical Sciences, National University of Rosario, Suipacha 570, S2002RLK, Rosario, Argentina
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Cites_doi	10.1016/0006-3002(62)90347-5 10.1002/bit.10135 10.1016/j.foodchem.2012.04.140 10.1002/jctb.280620313 10.1016/j.procbio.2009.02.009 10.1007/978-1-59745-324-0_3 10.1021/ma00234a031 10.1016/j.procbio.2009.04.007 10.1016/0168-1656(90)90112-O 10.1016/S0021-9258(19)50866-3 10.1021/ma061098q 10.1007/978-1-4757-2333-5 10.1021/ja01162a525 10.1016/j.ijbiomac.2011.05.012 10.1021/ma00027a047 10.1016/j.jcis.2008.12.048 10.1016/j.cocis.2004.09.006 10.1016/j.foodchem.2009.02.017 10.1002/app.11989 10.1016/j.foodhyd.2005.05.005 10.1016/j.procbio.2012.09.021 10.1021/la960653m 10.1021/ja01157a122 10.1021/bm050592j 10.1016/j.foodres.2013.06.009 10.1016/j.cocis.2005.05.007 10.1016/j.foodhyd.2008.04.008 10.1021/bm990006k 10.1016/j.jchromb.2008.07.029 10.1016/j.colsurfb.2006.10.003 10.1021/bp960013 10.1002/bit.10606 10.1016/j.bpc.2005.08.010 10.1016/j.chroma.2006.08.044 10.1016/j.idairyj.2006.05.009 10.1016/j.chroma.2004.10.018 10.1016/j.bbagen.2008.05.009 10.1016/j.carbpol.2012.01.019 10.1039/c2sm27002a 10.1085/jgp.19.6.991 10.1016/j.jchromb.2010.04.008 10.1016/j.ijbiomac.2012.10.014 10.1021/jp980486u 10.1002/jps.24025 10.1085/jgp.18.4.433 10.1007/s11224-009-9426-z 10.1021/bm025667n 10.1073/pnas.61.2.636 10.1016/j.seppur.2013.05.047 10.1016/j.seppur.2013.08.042 10.1021/la000648p 10.1021/bm049174p 10.1016/j.ijbiomac.2007.03.006 10.1021/bi00345a005
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References	Bohidar H, Dubin P, Majhi P, Tribet C and Jaeger W, Effects of protein-polyelectrolyte affinity and polyelectrolyte molecular weight on dynamic properties of bovine serum albumin-poly (diallyldimethylammonium chloride) coacervates. Biomacromolecules 6:1573 (2005). Weinbreck F, de Vries R, Schrooyen P and de Kruif CG, Complex coacervation of whey proteins and gum arabic. Biomacromolecules 4:293 (2003). Holler C, Vaughan D and Zhang C, Polyethyleneimine precipitation versus anion exchange chromatography in fractionating recombinant β-glucuronidase from transgenic tobacco extract. J Chromatog A 1142:98 (2007). Arakawa T and Timasheff SN, Mechanism of polyethylene glycol interaction with proteins. Biochemistry 24:6756 (1985). Cohn EJ, Gurd FRN, Surgenor DM, Barnes BA, Brown RK, Derouaux G et al., A system for the separation of the components of human blood: quantitative procedures for the separation of the protein components of human plasma1a,b,c. J Am Chem Soc 72:465 (1950). Kunitz M and Northrop JH, Isolation from beef pancreas of crystalline trypsinogen, trypsin, a trypsin inhibitor, and an inhibitor-trypsin compound. J Gen Physiol 19:991 (1936). Boeris V, Farruggia B and Pico G, Chitosan-bovine serum albumin complex formation: a model to design an enzyme isolation method by polyelectrolyte precipitation. J Chromatogr B Analyt Technol Biomed Life Sci 878:1543 (2010). Valetti NW, Boeris V and Picó G, Characterization of chymotrypsin-ι-carrageenan complex in aqueous solution: a solubility and thermodynamical stability study. Int J Biologic Macromolec 52:45 (2013). Grodzki AC and Berenstein E, in Immunocytochemical Methods and Protocols, ed. by Oliver C and Jamur CM. Humana Press, Totowa, NJ, pp. 15-26 (2010). Berdick M and Morawetz H, The interaction of catalase with synthetic polyelectrolytes. J Biol Chem 206:959 (1954). Harnsilawat T, Pongsawatmanit R and McClements D, Characterization of β-lactoglobulin-sodium alginate interactions in aqueous solutions: a calorimetry, light scattering, electrophoretic mobility and solubility study. Food Hydrocolloids 20:577 (2006). Sperber BLHM, Schols HA, Cohen Stuart MA, Norde W and Voragen AGJ, Influence of the overall charge and local charge density of pectin on the complex formation between pectin and β-lactoglobulin. Food Hydrocolloids 23:765 (2009). Kokufuta E, Shimizu H and Nakamura I, Stoichiometric complexation of human serum albumin with strongly acidic and basic polyelectrolytes. Macromolecules 15:1618 (1982). Menkhaus TJ, Eriksson SU, Whitson PB and Glatz CE, Host selection as a downstream strategy: polyelectrolyte precipitation of β-glucuronidase from plant extracts. Biotechnol Bioeng 77:148 (2002). Lombardi J, Woitovich Valetti N, Picó G and Boeris V, Obtainment of a highly concentrated pancreatic serine proteases extract from bovine pancreas by precipitation with polyacrylate. Sep Purif Technol 116:170 (2013). Schwert MH and Neurath H, The precipitation of insulin by thiocyanate1. J Am Chem Soc 72:2784 (1950). Morawetz H and Hughes WL, The interaction of proteins with synthetic polyelectrolytes. I. Complexing of bovine serum albumin. J Phys Chem 56:64 (1952). Doyle RJ, Woodside EE and Fishel CW, Protein-polyelectrolyte interactions. The concanavalin A precipitin reaction with polyelectrolytes and polysaccharide derivatives. Biochem J 106:35 (1968). Boeris V, Farruggia B, Nerli B, Romanini D and Picó G, Protein-flexible chain polymer interactions to explain protein partition in aqueous two-phase systems and the protein-polyelectrolyte complex formation. Int J Biol Macromol 41:286 (2007). Kunitz M and Northrop JH Crystalline chymo-trypsin and chymo-trypsinogen. Isolation, crystallization and general properties of a new proteolitic enzyme and its precursor. J Gen Physiol 18:433 (1935). Tejeda-Mansir A, Montesinos-Cisneros R and Guzmán R, Bioseparaciones. Editorial UNISON, México, 307 (1995). Zhang C, Lillie R, Cotter J and Vaughan D, Lysozyme purification from tobacco extract by polyelectrolyte precipitation. J Chromatog A 1069:107 (2005). Braia M, Porfiri MC, Farruggia B, Picó G and Romanini D, Complex formation between protein and poly vinyl sulfonate as a strategy of proteins isolation. J Chromatogr B 873:139 (2008). Boeris V, Spelzini D, Salgado JP, Picó G, Romanini D and Farruggia B, Chymotrypsin-poly vinyl sulfonate interaction studied by dynamic light scattering and turbidimetric approaches. Biochim Biophys Acta (BBA) - General Subjects 1780:1032 (2008). Stone AK, Cheung L, Chang C and Nickerson MT, Formation and functionality of soluble and insoluble electrostatic complexes within mixtures of canola protein isolate and (k-, ι-and λ-type) carrageenan. Food Res Int 54:195 (2013). Collins KD, Ion hydration: implications for cellular function, polyelectrolytes, and protein crystallization. Biophys Chem 119:271 (2006). Steward MW and Petty RE, The use of ammonium sulphate globulin precipitation for determination of affinity of anti-protein antibodies in mouse serum. Immunology 22:747 (1972). Duong-Ly KC and Gabelli SB, Methods in Enzymology, Volume 541,ed. by Jon L. Academic Press, pp. 85-94 (2014). Tsuboi A, Izumi T, Hirata M, Xia J, Dubin PL and Kokufuta E, Complexation of proteins with a strong polyanion in an aqueous salt-free system. Langmuir 12:6295 (1996). Hattori T, Hallberg R and Dubin PL, Roles of electrostatic interaction and polymer structure in the binding of β-lactoglobulin to anionic polyelectrolytes: measurement of binding constants by frontal analysis continuous capillary electrophoresis. Langmuir 16:9738 (2000). Bassani G, Farruggia B and Picó G, Cationic polyelectrolytes-lipases complexes formation as tool for recovery of these enzymes from their natural sources. Int J Biolog Macromol 49:351 (2011). Davoren PR, The isolation of insulin from a single cat pancreas. Biochim Biophys Acta 63:150 (1962). Kurinomaru T, Maruyama T, Izaki S, Handa K, Kimoto T and Shiraki K, Protein-poly (amino acid) complex precipitation for high-concentration protein formulation. J Pharmaceut Sci 103:2248 (2014). Montilla A et al., Isolation of bovine β-lactoglobulin from complexes with chitosan. Int Dairy J 17:459 (2007). Porfiri MC, Braia M, Farruggia B, Picó G and Romanini D, Precipitation with poly acrylic acid as a trypsin bioseparation strategy. Process Biochem 44:1046 (2009). Wang YF, Gao JY and Dubin PL, Protein separation via polyelectrolyte coacervation: selectivity and efficiency. Biotechnol Prog 12:356 (1996). Boeris V, Romanini D, Farruggia B and Picó G, Purification of chymotrypsin from bovine pancreas using precipitation with a strong anionic polyelectrolyte. Process Biochem 44:588 (2009). de Kruif CG, Weinbreck F and de Vries R, Complex coacervation of proteins and anionic polysaccharides. Current Opin Colloid & Interface Sci 9:340 (2004). Woitovich Valetti N, Lombardi J, Boeris V and Picó G, Precipitation of chymotrypsin from fresh bovine pancreas using ι-carrageenan. Process Biochem 47:2570 (2012). Matsunami H, Kikuchi R, Ogawa K and Kokufuta E, Light scattering study of complex formation between protein and polyelectrolyte at various ionic strengths. Colloids Surfaces B: Biointerfaces 56:142 (2007). Zhao J, Ford CF, Glatz CE, Rougvie MA and Gendel SM, Polyelectrolyte precipitation of β-galactosidase fusions containing poly-aspartic acid tails. J Biotechnol 14:273 (1990). Nath S, Complexation behavior of proteins with polyelectrolytes and random acrylic polyampholytes using turbidimetric titration. J Chem Technol Biotechnol 62:295 (1995). Park JM, Muhoberac BB, Dubin PL and Xia J, Effects of protein charge heterogeneity in protein-polyelectrolyte complexation. Macromolecules 25:290 (1992). Simsek-Ege FA, Bond GM and Stringer J, Polyelectrolyte complex formation between alginate and chitosan as a function of pH. J Appl Polym Sci 88:346 (2003). Sui Z, Jaber JA and Schlenoff JB, Polyelectrolyte complexes with pH-tunable solubility. Macromolecules 39:8145 (2006). Cooper CL, Dubin PL, Kayitmazer AB and Turksen S, Polyelectrolyte-protein complexes. Current Opin Colloid and Interface Sci 10:52 (2005). Kayitmazer AB, Seeman D, Minsky BB, Dubin PL and Xu Y, Protein-polyelectrolyte interactions. Soft Matter 9:2553 (2013). Cuatrecasas P, Wilchek M and Anfinsen CB, Selective enzyme purification by affinity chromatography. Proc Nat Acad Sci USA 61:636 (1968). Mattison KW, Dubin PL and Brittain IJ, Complex formation between bovine serum albumin and strong polyelectrolytes: effect of polymer charge density. J Phys Chem B 102:3830 (1998). Huang G-Q, Sun Y-T, Xiao J-X and Yang J, Complex coacervation of soybean protein isolate and chitosan. Food Chem 135:534 (2012). Woitovich Valetti N and Picó G, A friendly method for Raphanus sativus L (wild radish) peroxidase purification by polyelectrolyte precipitation. Sep Purif Technol 119:1 (2013). Castellan GW and Basín MEC, Fisicoquímica. Pearson Educación (1987). Kaibara K, Okazaki T, Bohidar HB and Dubin PL, pH-induced coacervation in complexes of bovine serum albumin and cationic polyelectrolytes. Biomacromolecules 1:100 (2000). Rinaudo M, Polyelectrolyte properties of a plant and animal polysaccharide. Structural Chem 20:277 (2009). Scopes RK, Protein Purification: Principles and Practice. Springer Advanced Texts in Chemistry, Springer-Verlag, New York (1994). Kamiya N and Klibanov AM, Controling the rate of protein release from polyelectrolyte complexes. Biotechnol Bioeng 82:590 (2003). Perez AA, Carrara CR, Sánchez CC, Patino JMR and Santiago LG, Interactions between milk whey protein and polysaccharide in solution. Food Chem 116:104 (2009). Cooper CL, Goulding A, Kayitmazer AB, Ulrich S, Stoll S, Turksen S et al., Effects of polyelectrolyte chain stiffness, charge mobility, and charge sequences on binding to proteins and micelles. Biomacromolecules 7:1025 (2006). Zhao Y, Li F, Carvajal MT and Harris MT, Interactions between bovine serum albumin and alginate: an evaluation of alginate as protein carrier. J Colloid Interface Sci 332:345 (2009). Ru Q, Wang Y, Lee J, Ding Y an 2009; 44 1982; 15 1990; 14 2007; 1142 2006; 39 2004; 9 2000; 1 1968; 61 1954; 206 2013; 9 2009; 116 1985; 24 1995; 62 2006; 20 2000; 16 2012; 135 2010; 878 2013; 54 2013; 119 2013; 116 1950; 72 2013; 52 1987 2003; 4 2008; 873 2003; 82 2003; 88 1936; 19 2009; 23 2007; 17 1952; 56 1968; 106 2006; 119 2009; 20 2010 2002; 77 2006; 7 2009; 332 1995 1994 1972; 22 2007; 56 1935; 18 1996; 12 2008; 1780 2005; 10 2005; 6 1992; 25 2014 2007; 41 1962; 63 2012; 47 2011; 49 1998; 102 2012; 88 2014; 103 2005; 1069 e_1_2_7_5_1 e_1_2_7_7_1 e_1_2_7_19_1 e_1_2_7_60_1 e_1_2_7_15_1 e_1_2_7_41_1 e_1_2_7_13_1 Morawetz H (e_1_2_7_16_1) 1952; 56 e_1_2_7_43_1 Castellan GW (e_1_2_7_45_1) 1987 e_1_2_7_11_1 e_1_2_7_47_1 e_1_2_7_26_1 e_1_2_7_49_1 e_1_2_7_28_1 e_1_2_7_50_1 e_1_2_7_25_1 e_1_2_7_31_1 e_1_2_7_52_1 e_1_2_7_23_1 e_1_2_7_33_1 e_1_2_7_54_1 e_1_2_7_21_1 e_1_2_7_35_1 e_1_2_7_56_1 e_1_2_7_58_1 e_1_2_7_39_1 e_1_2_7_6_1 e_1_2_7_4_1 Doyle RJ (e_1_2_7_17_1) 1968; 106 e_1_2_7_8_1 e_1_2_7_18_1 e_1_2_7_40_1 e_1_2_7_61_1 e_1_2_7_2_1 e_1_2_7_14_1 e_1_2_7_42_1 e_1_2_7_12_1 e_1_2_7_44_1 e_1_2_7_10_1 e_1_2_7_46_1 e_1_2_7_48_1 e_1_2_7_27_1 e_1_2_7_29_1 Tejeda‐Mansir A (e_1_2_7_37_1) 1995 e_1_2_7_51_1 e_1_2_7_30_1 e_1_2_7_53_1 Steward MW (e_1_2_7_3_1) 1972; 22 e_1_2_7_24_1 e_1_2_7_32_1 e_1_2_7_55_1 e_1_2_7_22_1 e_1_2_7_34_1 e_1_2_7_57_1 e_1_2_7_20_1 e_1_2_7_36_1 e_1_2_7_59_1 Duong‐Ly KC (e_1_2_7_9_1) 2014 e_1_2_7_38_1
References_xml	– volume: 61 start-page: 636 year: 1968 article-title: Selective enzyme purification by affinity chromatography publication-title: Proc Nat Acad Sci USA – volume: 1 start-page: 100 year: 2000 article-title: pH‐induced coacervation in complexes of bovine serum albumin and cationic polyelectrolytes publication-title: Biomacromolecules – volume: 15 start-page: 1618 year: 1982 article-title: Stoichiometric complexation of human serum albumin with strongly acidic and basic polyelectrolytes publication-title: Macromolecules – start-page: 307 year: 1995 – volume: 7 start-page: 1025 year: 2006 article-title: Effects of polyelectrolyte chain stiffness, charge mobility, and charge sequences on binding to proteins and micelles publication-title: Biomacromolecules – volume: 49 start-page: 351 year: 2011 article-title: Cationic polyelectrolytes–lipases complexes formation as tool for recovery of these enzymes from their natural sources publication-title: Int J Biolog Macromol – volume: 12 start-page: 356 year: 1996 article-title: Protein separation via polyelectrolyte coacervation: selectivity and efficiency publication-title: Biotechnol Prog – volume: 22 start-page: 747 year: 1972 article-title: The use of ammonium sulphate globulin precipitation for determination of affinity of anti‐protein antibodies in mouse serum publication-title: Immunology – volume: 12 start-page: 6295 year: 1996 article-title: Complexation of proteins with a strong polyanion in an aqueous salt‐free system publication-title: Langmuir – volume: 52 start-page: 45 year: 2013 article-title: Characterization of chymotrypsin–ι‐carrageenan complex in aqueous solution: a solubility and thermodynamical stability study publication-title: Int J Biologic Macromolec – volume: 44 start-page: 588 year: 2009 article-title: Purification of chymotrypsin from bovine pancreas using precipitation with a strong anionic polyelectrolyte publication-title: Process Biochem – year: 1994 – volume: 873 start-page: 139 year: 2008 article-title: Complex formation between protein and poly vinyl sulfonate as a strategy of proteins isolation publication-title: J Chromatogr B – volume: 54 start-page: 195 year: 2013 article-title: Formation and functionality of soluble and insoluble electrostatic complexes within mixtures of canola protein isolate and (k‐, ι‐and λ‐type) carrageenan publication-title: Food Res Int – volume: 25 start-page: 290 year: 1992 article-title: Effects of protein charge heterogeneity in protein‐polyelectrolyte complexation publication-title: Macromolecules – volume: 39 start-page: 8145 year: 2006 article-title: Polyelectrolyte complexes with pH‐tunable solubility publication-title: Macromolecules – volume: 119 start-page: 1 year: 2013 article-title: A friendly method for L (wild radish) peroxidase purification by polyelectrolyte precipitation publication-title: Sep Purif Technol – volume: 41 start-page: 286 year: 2007 article-title: Protein‐flexible chain polymer interactions to explain protein partition in aqueous two‐phase systems and the protein–polyelectrolyte complex formation publication-title: Int J Biol Macromol – volume: 6 start-page: 1573 year: 2005 article-title: Effects of protein‐polyelectrolyte affinity and polyelectrolyte molecular weight on dynamic properties of bovine serum albumin‐poly (diallyldimethylammonium chloride) coacervates publication-title: Biomacromolecules – volume: 106 issue: 35 year: 1968 article-title: Protein–polyelectrolyte interactions. The concanavalin A precipitin reaction with polyelectrolytes and polysaccharide derivatives publication-title: Biochem J – volume: 206 start-page: 959 year: 1954 article-title: The interaction of catalase with synthetic polyelectrolytes publication-title: J Biol Chem – volume: 9 start-page: 340 year: 2004 article-title: Complex coacervation of proteins and anionic polysaccharides publication-title: Current Opin Colloid & Interface Sci – volume: 23 start-page: 765 year: 2009 article-title: Influence of the overall charge and local charge density of pectin on the complex formation between pectin and β‐lactoglobulin publication-title: Food Hydrocolloids – volume: 77 start-page: 148 year: 2002 article-title: Host selection as a downstream strategy: polyelectrolyte precipitation of β‐glucuronidase from plant extracts publication-title: Biotechnol Bioeng – volume: 72 start-page: 465 year: 1950 article-title: A system for the separation of the components of human blood: quantitative procedures for the separation of the protein components of human plasma1a,b,c publication-title: J Am Chem Soc – volume: 878 start-page: 1543 year: 2010 article-title: Chitosan‐bovine serum albumin complex formation: a model to design an enzyme isolation method by polyelectrolyte precipitation publication-title: J Chromatogr B Analyt Technol Biomed Life Sci – volume: 88 start-page: 346 year: 2003 article-title: Polyelectrolyte complex formation between alginate and chitosan as a function of pH publication-title: J Appl Polym Sci – volume: 44 start-page: 1046 year: 2009 article-title: Precipitation with poly acrylic acid as a trypsin bioseparation strategy publication-title: Process Biochem – volume: 10 start-page: 52 year: 2005 article-title: Polyelectrolyte–protein complexes publication-title: Current Opin Colloid and Interface Sci – volume: 20 start-page: 277 year: 2009 article-title: Polyelectrolyte properties of a plant and animal polysaccharide publication-title: Structural Chem – volume: 56 issue: 64 year: 1952 article-title: The interaction of proteins with synthetic polyelectrolytes. I. Complexing of bovine serum albumin publication-title: J Phys Chem – volume: 1780 start-page: 1032 year: 2008 article-title: Chymotrypsin–poly vinyl sulfonate interaction studied by dynamic light scattering and turbidimetric approaches publication-title: Biochim Biophys Acta (BBA) ‐ General Subjects – volume: 88 start-page: 838 year: 2012 article-title: Turbidity and rheological properties of bovine serum albumin/pectin coacervates: effect of salt concentration and initial protein/polysaccharide ratio publication-title: Carbohydrate Polymers – volume: 20 start-page: 577 year: 2006 article-title: Characterization of β‐lactoglobulin–sodium alginate interactions in aqueous solutions: a calorimetry, light scattering, electrophoretic mobility and solubility study publication-title: Food Hydrocolloids – year: 1987 article-title: Fisicoquímica publication-title: Pearson Educación – volume: 18 start-page: 433 year: 1935 article-title: Isolation, crystallization and general properties of a new proteolitic enzyme and its precursor publication-title: J Gen Physiol – volume: 119 start-page: 271 year: 2006 article-title: Ion hydration: implications for cellular function, polyelectrolytes, and protein crystallization publication-title: Biophys Chem – volume: 82 start-page: 590 year: 2003 article-title: Controling the rate of protein release from polyelectrolyte complexes publication-title: Biotechnol Bioeng – volume: 62 start-page: 295 year: 1995 article-title: Complexation behavior of proteins with polyelectrolytes and random acrylic polyampholytes using turbidimetric titration publication-title: J Chem Technol Biotechnol – volume: 63 start-page: 150 year: 1962 article-title: The isolation of insulin from a single cat pancreas publication-title: Biochim Biophys Acta – volume: 17 start-page: 459 year: 2007 article-title: Isolation of bovine β‐lactoglobulin from complexes with chitosan publication-title: Int Dairy J – volume: 102 start-page: 3830 year: 1998 article-title: Complex formation between bovine serum albumin and strong polyelectrolytes: effect of polymer charge density publication-title: J Phys Chem B – volume: 1069 start-page: 107 year: 2005 article-title: Lysozyme purification from tobacco extract by polyelectrolyte precipitation publication-title: J Chromatog A – volume: 47 start-page: 2570 year: 2012 article-title: Precipitation of chymotrypsin from fresh bovine pancreas using ι‐carrageenan publication-title: Process Biochem – volume: 135 start-page: 534 year: 2012 article-title: Complex coacervation of soybean protein isolate and chitosan publication-title: Food Chem – volume: 14 start-page: 273 year: 1990 article-title: Polyelectrolyte precipitation of β‐galactosidase fusions containing poly‐aspartic acid tails publication-title: J Biotechnol – volume: 56 start-page: 142 year: 2007 article-title: Light scattering study of complex formation between protein and polyelectrolyte at various ionic strengths publication-title: Colloids Surfaces B: Biointerfaces – start-page: 15 year: 2010 end-page: 26 – volume: 72 start-page: 2784 year: 1950 article-title: The precipitation of insulin by thiocyanate1 publication-title: J Am Chem Soc – volume: 103 start-page: 2248 year: 2014 article-title: Protein–poly (amino acid) complex precipitation for high‐concentration protein formulation publication-title: J Pharmaceut Sci – volume: 116 start-page: 170 year: 2013 article-title: Obtainment of a highly concentrated pancreatic serine proteases extract from bovine pancreas by precipitation with polyacrylate publication-title: Sep Purif Technol – volume: 116 start-page: 104 year: 2009 article-title: Interactions between milk whey protein and polysaccharide in solution publication-title: Food Chem – volume: 16 start-page: 9738 year: 2000 article-title: Roles of electrostatic interaction and polymer structure in the binding of β‐lactoglobulin to anionic polyelectrolytes: measurement of binding constants by frontal analysis continuous capillary electrophoresis publication-title: Langmuir – volume: 9 start-page: 2553 year: 2013 article-title: Protein‐polyelectrolyte interactions publication-title: Soft Matter – volume: 1142 start-page: 98 year: 2007 article-title: Polyethyleneimine precipitation versus anion exchange chromatography in fractionating recombinant β‐glucuronidase from transgenic tobacco extract publication-title: J Chromatog A – volume: 24 start-page: 6756 year: 1985 article-title: Mechanism of polyethylene glycol interaction with proteins publication-title: Biochemistry – start-page: 85 year: 2014 end-page: 94 – volume: 332 start-page: 345 year: 2009 article-title: Interactions between bovine serum albumin and alginate: an evaluation of alginate as protein carrier publication-title: J Colloid Interface Sci – volume: 19 start-page: 991 year: 1936 article-title: Isolation from beef pancreas of crystalline trypsinogen, trypsin, a trypsin inhibitor, and an inhibitor‐trypsin compound publication-title: J Gen Physiol – volume: 4 start-page: 293 year: 2003 article-title: Complex coacervation of whey proteins and gum arabic publication-title: Biomacromolecules – ident: e_1_2_7_2_1 doi: 10.1016/0006-3002(62)90347-5 – ident: e_1_2_7_55_1 doi: 10.1002/bit.10135 – start-page: 85 volume-title: Methods in Enzymology year: 2014 ident: e_1_2_7_9_1 contributor: fullname: Duong‐Ly KC – ident: e_1_2_7_47_1 doi: 10.1016/j.foodchem.2012.04.140 – ident: e_1_2_7_28_1 doi: 10.1002/jctb.280620313 – ident: e_1_2_7_13_1 doi: 10.1016/j.procbio.2009.02.009 – ident: e_1_2_7_10_1 doi: 10.1007/978-1-59745-324-0_3 – ident: e_1_2_7_21_1 doi: 10.1021/ma00234a031 – ident: e_1_2_7_34_1 doi: 10.1016/j.procbio.2009.04.007 – ident: e_1_2_7_59_1 doi: 10.1016/0168-1656(90)90112-O – volume: 106 issue: 35 year: 1968 ident: e_1_2_7_17_1 article-title: Protein–polyelectrolyte interactions. The concanavalin A precipitin reaction with polyelectrolytes and polysaccharide derivatives publication-title: Biochem J contributor: fullname: Doyle RJ – ident: e_1_2_7_18_1 doi: 10.1016/S0021-9258(19)50866-3 – ident: e_1_2_7_25_1 doi: 10.1021/ma061098q – ident: e_1_2_7_6_1 doi: 10.1007/978-1-4757-2333-5 – ident: e_1_2_7_8_1 doi: 10.1021/ja01162a525 – volume: 56 issue: 64 year: 1952 ident: e_1_2_7_16_1 article-title: The interaction of proteins with synthetic polyelectrolytes. I. Complexing of bovine serum albumin publication-title: J Phys Chem contributor: fullname: Morawetz H – ident: e_1_2_7_52_1 doi: 10.1016/j.ijbiomac.2011.05.012 – ident: e_1_2_7_41_1 doi: 10.1021/ma00027a047 – ident: e_1_2_7_24_1 doi: 10.1016/j.jcis.2008.12.048 – ident: e_1_2_7_15_1 doi: 10.1016/j.cocis.2004.09.006 – volume: 22 start-page: 747 year: 1972 ident: e_1_2_7_3_1 article-title: The use of ammonium sulphate globulin precipitation for determination of affinity of anti‐protein antibodies in mouse serum publication-title: Immunology contributor: fullname: Steward MW – ident: e_1_2_7_50_1 doi: 10.1016/j.foodchem.2009.02.017 – ident: e_1_2_7_19_1 doi: 10.1002/app.11989 – ident: e_1_2_7_44_1 doi: 10.1016/j.foodhyd.2005.05.005 – ident: e_1_2_7_22_1 doi: 10.1016/j.procbio.2012.09.021 – ident: e_1_2_7_14_1 doi: 10.1021/la960653m – ident: e_1_2_7_5_1 doi: 10.1021/ja01157a122 – ident: e_1_2_7_53_1 doi: 10.1021/bm050592j – ident: e_1_2_7_54_1 doi: 10.1016/j.foodres.2013.06.009 – ident: e_1_2_7_20_1 doi: 10.1016/j.cocis.2005.05.007 – ident: e_1_2_7_26_1 doi: 10.1016/j.foodhyd.2008.04.008 – ident: e_1_2_7_31_1 doi: 10.1021/bm990006k – ident: e_1_2_7_12_1 doi: 10.1016/j.jchromb.2008.07.029 – ident: e_1_2_7_32_1 doi: 10.1016/j.colsurfb.2006.10.003 – ident: e_1_2_7_42_1 doi: 10.1021/bp960013 – ident: e_1_2_7_30_1 doi: 10.1002/bit.10606 – ident: e_1_2_7_61_1 doi: 10.1016/j.bpc.2005.08.010 – ident: e_1_2_7_48_1 doi: 10.1016/j.chroma.2006.08.044 – ident: e_1_2_7_49_1 doi: 10.1016/j.idairyj.2006.05.009 – ident: e_1_2_7_46_1 doi: 10.1016/j.chroma.2004.10.018 – ident: e_1_2_7_27_1 doi: 10.1016/j.bbagen.2008.05.009 – ident: e_1_2_7_33_1 doi: 10.1016/j.carbpol.2012.01.019 – ident: e_1_2_7_40_1 doi: 10.1039/c2sm27002a – start-page: 307 volume-title: Bioseparaciones year: 1995 ident: e_1_2_7_37_1 contributor: fullname: Tejeda‐Mansir A – ident: e_1_2_7_11_1 doi: 10.1085/jgp.19.6.991 – ident: e_1_2_7_23_1 doi: 10.1016/j.jchromb.2010.04.008 – ident: e_1_2_7_35_1 doi: 10.1016/j.ijbiomac.2012.10.014 – ident: e_1_2_7_38_1 doi: 10.1021/jp980486u – ident: e_1_2_7_36_1 doi: 10.1002/jps.24025 – ident: e_1_2_7_7_1 doi: 10.1085/jgp.18.4.433 – ident: e_1_2_7_51_1 doi: 10.1007/s11224-009-9426-z – ident: e_1_2_7_39_1 doi: 10.1021/bm025667n – ident: e_1_2_7_4_1 doi: 10.1073/pnas.61.2.636 – ident: e_1_2_7_57_1 doi: 10.1016/j.seppur.2013.05.047 – ident: e_1_2_7_58_1 doi: 10.1016/j.seppur.2013.08.042 – ident: e_1_2_7_29_1 doi: 10.1021/la000648p – year: 1987 ident: e_1_2_7_45_1 article-title: Fisicoquímica publication-title: Pearson Educación contributor: fullname: Castellan GW – ident: e_1_2_7_43_1 doi: 10.1021/bm049174p – ident: e_1_2_7_56_1 doi: 10.1016/j.ijbiomac.2007.03.006 – ident: e_1_2_7_60_1 doi: 10.1021/bi00345a005
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Snippet	Complexation between proteins and polyelectrolytes through electrostatic interactions gives either soluble or non‐soluble complexes, leading to phase... Abstract Complexation between proteins and polyelectrolytes through electrostatic interactions gives either soluble or non‐soluble complexes, leading to phase... Complexation between proteins and polyelectrolytes through electrostatic interactions gives either soluble or non-soluble complexes, leading to phase...
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SubjectTerms	bioseparation Chromium downstream processes downstream processes, bioseparation Electrostatics enzyme purification Enzymes Phase separation Polyelectrolytes Precipitation (chemistry) Proteins Scaling up
Title	Polyelectrolytes-protein complexes: a viable platform in the downstream processes of industrial enzymes at scaling up level
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