Partitioning of glutenin flour of special wheat using aqueous two-phase systems |
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| Authors: | Ingrid Silva Barberino do Nascimento,Jane Sé lia dos Reis Coimbra,Joã o Paulo Martins,Luis Henrique Mendes da Silva,Renata Cristina Ferreira Bonomo,Mô nica Ribeiro Pirozzi,Aline Cinquini |
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| Affiliation: | 1. State University of the Southwest of Bahia (UESB), Primavera Square, Number 40, 45700-000 Itapetinga, BA, Brazil;2. Department of Food Technology, Federal University of Viçosa (UFV), P. H. Rolfs Av., s/n, 36570-000 Viçosa, MG, Brazil;3. Federal Institute of North of Minas Gerais (IFNMG), MG 202, km 407, 38.680-000 Arinos, MG, Brazil;4. Department of Chemistry, Federal University of Viçosa (UFV), P. H. Rolfs Av., s/n, 36570-000 Viçosa, MG, Brazil |
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| Abstract: | The partitioning behavior of the glutenin proteins was evaluated in aqueous two-phase systems (ATPSs) formed by sulfate salts (lithium or sodium) and poly(ethylene glycol) (PEG) with average molar mass of 1500 g mol−1 or 4000 g mol−1. The partition coefficients for the glutenin proteins in each ATPS were investigated as a function of the temperature (278.2 K–318.2 K), tie line length (TLL) and electrolyte nature. In all ATPS, the majority of glutenin proteins spontaneously concentrate in the polymer-rich phase (Kp > 1). The partition coefficient is very dependent on the salt nature and the ATPS formed by PEG + lithium sulfate presents higher Kp values as compared with the ATPS formed PEG + sodium sulfate. An increase of molar mass of polymer promotes a decrease of Kp. Thermodynamic parameters of transfer (ΔtrG, ΔtrH and ΔtrS) were obtained by the application of the Van’t Hoff equation (VHE). The values obtained by VHE indicate that the transfer of glutenin proteins to the polymer-rich phase has an enthalpic origin. |
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| Keywords: | Aqueous two-phase systems Glutenin Poly(ethylene glycol) |
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