Whey protein interactions in acidic cold-set gels at different pH values

dc.creatorCavallieri, ALF
dc.creatorCosta-Netto, AP
dc.creatorMenossi, M
dc.creatorDa Cunha, RL
dc.date2007
dc.dateNOV-DEC
dc.date2014-11-18T09:13:41Z
dc.date2015-11-26T16:53:23Z
dc.date2014-11-18T09:13:41Z
dc.date2015-11-26T16:53:23Z
dc.date.accessioned2018-03-28T23:40:29Z
dc.date.available2018-03-28T23:40:29Z
dc.identifierLait. Edp Sciences S A, v. 87, n. 6, n. 535, n. 554, 2007.
dc.identifier0023-7302
dc.identifierWOS:000252134200004
dc.identifier10.1051/lait:2007032
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/72859
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/72859
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/72859
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1276566
dc.descriptionCold-set whey protein isolate gels (7% w/w) were produced by the addition of different amounts of glucono-delta-lactone to thermally denatured protein solutions. After 48 h of incubation at 10 degrees C, different final pH values were obtained (5.2 to 3.9). The gels were analysed by uniaxial compression measurements, water-holding capacity and protein solubility. The water-holding capacity of the gels decreased at pH values near the pI, this being associated with the lower protein solubility at this pH value. Protein solubility in the presence or absence of denaturing and reducing agents indicated that electrostatic interactions were responsible for the maintenance of the acidified gel structure at pH values from 5.2 to 4.6, but at pH 4.2, more hydrophobic interactions were present in relation to other final gel pHs, in spite of beta-lactoglobulin (beta-Lg) and BSA being far from their pI values. Complementary PAGE assays showed that disulphide bonds were associated with internal stabilisation of the protein aggregates formed during heat treatment. The mechanical properties of the gels were influenced by the final system pH value, showing that the strongest network was observed at pH 5.2. The results allowed the conclusion that although the interactions amongst the aggregates in the network of cold-set whey protein gels were essentially the same at the pH values evaluated, beta-Lg played an important role in gel stabilisation due to its high concentration in WPI, strengthening the structure at its pI and, at the same time, providing good water-retention capacity.
dc.description87
dc.description6
dc.description535
dc.description554
dc.languageen
dc.publisherEdp Sciences S A
dc.publisherLes Ulis Cedex A
dc.publisherFrança
dc.relationLait
dc.relationLait
dc.rightsfechado
dc.sourceWeb of Science
dc.subjectwhey proteins
dc.subjectglucono-delta-lactone
dc.subjectcold gelation
dc.subjectprotein interactions
dc.subjectHeat-induced Aggregation
dc.subjectBeta-lactoglobulin-b
dc.subjectAlpha-lactalbumin
dc.subjectIsoelectric Precipitation
dc.subjectFunctional-properties
dc.subjectGelation
dc.subjectConcentrate
dc.subjectIsolate
dc.subjectDisulfide
dc.titleWhey protein interactions in acidic cold-set gels at different pH values
dc.typeArtículos de revistas


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