Gelation of β-lactoglobulin in the presence of propylene glycol alginate: Kinetics and gel properties
The role of the non-gelling polysaccharide, propyleneglycol alginate (PGA), on the dynamics of gelation and gel properties of β-lactoglobulin (β-lg) under conditions where the protein alone does not gel (6%) was analyzed. To this end, the kinetics of gelation, aggregation and denaturation of β-lg in...
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Elsevier
2003
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| Acceso en línea: | Registro en Scopus DOI Handle Registro en la Biblioteca Digital |
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| LEADER | 09024caa a22012257a 4500 | ||
|---|---|---|---|
| 001 | PAPER-4864 | ||
| 003 | AR-BaUEN | ||
| 005 | 20230518203427.0 | ||
| 008 | 190411s2003 xx ||||fo|||| 00| 0 eng|d | ||
| 024 | 7 | |2 scopus |a 2-s2.0-0041660904 | |
| 024 | 7 | |2 cas |a alginic acid propylene glycol ester, 9005-37-2; beta lactoglobulin, 9045-23-2 | |
| 040 | |a Scopus |b spa |c AR-BaUEN |d AR-BaUEN | ||
| 030 | |a CSBBE | ||
| 100 | 1 | |a Baeza, R. | |
| 245 | 1 | 0 | |a Gelation of β-lactoglobulin in the presence of propylene glycol alginate: Kinetics and gel properties |
| 260 | |b Elsevier |c 2003 | ||
| 270 | 1 | 0 | |m Pilosof, A.M.R.; Departamento de Industrias, Fac. de Ciencias Exactas y Naturales, Ciudad Universitaria Nunez, Buenos Aires 1428, Argentina; email: apilosof@di.fcen.uba.ar |
| 506 | |2 openaire |e Política editorial | ||
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| 520 | 3 | |a The role of the non-gelling polysaccharide, propyleneglycol alginate (PGA), on the dynamics of gelation and gel properties of β-lactoglobulin (β-lg) under conditions where the protein alone does not gel (6%) was analyzed. To this end, the kinetics of gelation, aggregation and denaturation of β-lg in the mixed systems (pH 7) were studied at different temperatures (64-88°C). The presence of PGA increased thermal stability of β-lg. The rate of β-lg denaturation was decreased and the onset and peak denaturation temperatures increased by 2.2-2.4°C. PGA promoted the formation of larger aggregates that continued to grow in time. An average aggregate diameter of approximately 300 nm is reached at the gel point in the mixed β-lg+PGA systems, irrespective of the heating temperature. Comparing the activation energies for the aggregation (193 kJ/mol), denaturation (422 kJ/mol) and formation of the primary gel structure (1/tgel) (256 kJ/mol) processes in the mixed protein-polysaccharide system, it can be concluded that the rate determining step in the formation of the primary gel structure would be the aggregation of protein. Ea values for the processes after the gel point (solid phase gelation) suggest a diffusion limited process because of the high viscosity of the solid gelling matrix. The characteristics of the mixed β-lg+PGA gels in terms of rheological and textural parameters, water loss and microstructure were studied as a function of heating temperature and time. The extent of aggregation and the type of interactions involved, prior to denaturation seem to be very important in determining the gel structure and its properties. © 2003 Elsevier B.V. All rights reserved. |l eng | |
| 536 | |a Detalles de la financiación: Agencia Nacional de Promoción Científica y Tecnológica | ||
| 536 | |a Detalles de la financiación: Universidad Nacional del Litoral | ||
| 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, Universidad Nacional del Litoral, Consejo Nacional de Investigaciones Cientificas y Tecnicas y Agencia Nacional de Promocibn Cientifica y Tecnológica de la República Argentina. | ||
| 593 | |a Departamento de Industrias, Fac. de Ciencias Exactas y Naturales, Ciudad Universitaria Nunez, Buenos Aires 1428, Argentina | ||
| 593 | |a INTEC, Güemes 3450-3000 Santa Fe, Argentina | ||
| 690 | 1 | 0 | |a AGGREGATION |
| 690 | 1 | 0 | |a DENATURATION |
| 690 | 1 | 0 | |a GELATION |
| 690 | 1 | 0 | |a KINETICS |
| 690 | 1 | 0 | |a THERMODYNAMIC INCOMPATIBILITY |
| 690 | 1 | 0 | |a AGGLOMERATION |
| 690 | 1 | 0 | |a GELATION |
| 690 | 1 | 0 | |a GELS |
| 690 | 1 | 0 | |a HEATING |
| 690 | 1 | 0 | |a PROTEINS |
| 690 | 1 | 0 | |a DENATURATION |
| 690 | 1 | 0 | |a ALCOHOLS |
| 690 | 1 | 0 | |a ALGINIC ACID PROPYLENE GLYCOL ESTER |
| 690 | 1 | 0 | |a BETA LACTOGLOBULIN |
| 690 | 1 | 0 | |a POLYSACCHARIDE |
| 690 | 1 | 0 | |a CONFERENCE PAPER |
| 690 | 1 | 0 | |a FOOD ANALYSIS |
| 690 | 1 | 0 | |a FOOD PROCESSING |
| 690 | 1 | 0 | |a GEL |
| 690 | 1 | 0 | |a GELATION |
| 690 | 1 | 0 | |a KINETICS |
| 690 | 1 | 0 | |a MOLECULAR DYNAMICS |
| 690 | 1 | 0 | |a PRIORITY JOURNAL |
| 690 | 1 | 0 | |a PROTEIN AGGREGATION |
| 690 | 1 | 0 | |a PROTEIN ANALYSIS |
| 690 | 1 | 0 | |a PROTEIN DENATURATION |
| 690 | 1 | 0 | |a PROTEIN INTERACTION |
| 690 | 1 | 0 | |a PROTEIN STRUCTURE |
| 690 | 1 | 0 | |a TEMPERATURE |
| 690 | 1 | 0 | |a THERMOSTABILITY |
| 700 | 1 | |a Gugliotta, L.M. | |
| 700 | 1 | |a Pilosof, A.M.R. | |
| 773 | 0 | |d Elsevier, 2003 |g v. 31 |h pp. 81-93 |k n. 1-4 |p Colloids Surf. B Biointerfaces |x 09277765 |w (AR-BaUEN)CENRE-4236 |t Colloids and Surfaces B: Biointerfaces | |
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| 856 | 4 | 0 | |u https://hdl.handle.net/20.500.12110/paper_09277765_v31_n1-4_p81_Baeza |y Handle |
| 856 | 4 | 0 | |u https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09277765_v31_n1-4_p81_Baeza |y Registro en la Biblioteca Digital |
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