Influence of complexing carboxymethylcellulose on the thermostability and gelation of α-lactalbumin and β-lactoglobulin
Thermostability and gelation of the main proteins of whey, α-lactalbumin (α-lac) and β-lactoglobulin (β-lg) recovered by selective complexation with carboxymethylcellulose (CMC) was studied to evaluate its functionality in food systems. Their behavior was compared to the non-complexed proteins. Both...
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2007
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| LEADER | 14539caa a22011177a 4500 | ||
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| 001 | PAPER-6242 | ||
| 003 | AR-BaUEN | ||
| 005 | 20230518203555.0 | ||
| 008 | 190411s2007 xx ||||fo|||| 00| 0 eng|d | ||
| 024 | 7 | |2 scopus |a 2-s2.0-34248355091 | |
| 040 | |a Scopus |b spa |c AR-BaUEN |d AR-BaUEN | ||
| 030 | |a FOHYE | ||
| 100 | 1 | |a Capitani, C. | |
| 245 | 1 | 0 | |a Influence of complexing carboxymethylcellulose on the thermostability and gelation of α-lactalbumin and β-lactoglobulin |
| 260 | |c 2007 | ||
| 270 | 1 | 0 | |m Pilosof, A.M.R.; Departamento de Industrias, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Ciudad Universitaria, 1428 Buenos Aires, Argentina; email: apilosof@di.fcen.uba.ar |
| 506 | |2 openaire |e Política editorial | ||
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| 520 | 3 | |a Thermostability and gelation of the main proteins of whey, α-lactalbumin (α-lac) and β-lactoglobulin (β-lg) recovered by selective complexation with carboxymethylcellulose (CMC) was studied to evaluate its functionality in food systems. Their behavior was compared to the non-complexed proteins. Both complexes showed a maximum stability at pH 4, that is close to the pH of obtention of β-lg/CMC coacervate (pH 4) and α-lac/CMC coacervate (pH 3.2). Protein complexation increased the thermostability of β-lg by approximately 6-8 °C and that of α-lac by approximately 26 °C due to immobilization of protein molecules in a complex, mainly by electrostatic interactions and because of different amounts of bound polysaccharide. The denaturation enthalpy of complexed proteins markedly decreased as compared to free proteins. Storage modulus (G′) and loss modulus (G″) were recorded to reflect the structure development during heating β-lg/CMC and α-lac/CMC complexes at different pH values. β-lg/CMC complex at 20 wt% was a viscoelastic liquid at pH values within 2 and 8 but upon heating turned to a particulate viscoelastic gel. However, α-lac/CMC complex formed before heating opaque, large visible white particulate aggregates that sticked together to give a solid viscoelastic structure that was not further modified by thermal processing. © 2006 Elsevier Ltd. All rights reserved. |l eng | |
| 536 | |a Detalles de la financiación: Agencia Nacional de Promoción Científica y Tecnológica | ||
| 536 | |a Detalles de la financiación: Consejo Nacional de Investigaciones Científicas y Técnicas | ||
| 536 | |a Detalles de la financiación: Universidad de Buenos Aires | ||
| 536 | |a Detalles de la financiación: The authors acknowledge the financial support from Universidad de Buenos Aires, Agencia Nacional de Promoción Científica y Tecnológica and Consejo Nacional de Investigaciones Científicas y Técnicas de la República Argentina. We thank CYTED Project XI-17 and A.1.2 for supporting cooperation between Argentina and Brazil. | ||
| 593 | |a Facultade de Ciencias Farmaceuticas, Universidade de Sao Paulo, Cidade Universitaria, Sao Paulo, Brazil | ||
| 593 | |a Departamento de Industrias, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Ciudad Universitaria, 1428 Buenos Aires, Argentina | ||
| 593 | |a Members of Consejo Nacional de Investigaciones Cientificas y Tecnicas de la Republica, Argentina | ||
| 593 | |a Instituto de Tecnología de Alimentos, Centro de Química e Nutricao Aplicada, Campinas, SP, Brazil | ||
| 690 | 1 | 0 | |a COACERVATE |
| 690 | 1 | 0 | |a DENATURATION |
| 690 | 1 | 0 | |a DIFFERENTIAL SCANNING CALORIMETRY |
| 690 | 1 | 0 | |a GELS |
| 690 | 1 | 0 | |a PROTEIN POLYSACCHARIDE INTERACTIONS |
| 700 | 1 | |a Pérez, Oscar.E. | |
| 700 | 1 | |a Pacheco, B. | |
| 700 | 1 | |a Teresa, M. | |
| 700 | 1 | |a Pilosof, A.M.R. | |
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