Whey Protein/Arabic Gum Gels Formed by Chemical or Physical Gelation Process

dc.creatorValim, MD
dc.creatorCavallieri, ALF
dc.creatorCunha, RL
dc.date2009
dc.dateMAR
dc.date2014-11-18T09:14:29Z
dc.date2015-11-26T16:53:26Z
dc.date2014-11-18T09:14:29Z
dc.date2015-11-26T16:53:26Z
dc.date.accessioned2018-03-28T23:40:33Z
dc.date.available2018-03-28T23:40:33Z
dc.identifierFood Biophysics. Springer, v. 4, n. 1, n. 23, n. 31, 2009.
dc.identifier1557-1858
dc.identifierWOS:000263075100003
dc.identifier10.1007/s11483-008-9098-z
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/72860
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/72860
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/72860
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1276582
dc.descriptionWhey proteins (WP) gelation process with addition of Arabic gum (AG) was studied. Two different driving processes were employed to induce gelation: (1) heating of 12% whey protein isolate (WPI) solutions (w/w) or (2) acidification of previous thermal denatured WPI solutions (5% w/w) with glucono-delta-lactone (GDL). Protein concentrations were different because they were minimal to form gel in these two processes, but denaturation conditions were the same (90 A degrees C/30 min). Water-holding capacity and mechanical properties of the gels were evaluated. The BST equation was used to evaluate the nonlinear part of the stress-strain data. Cold-set gels were weaker than heat-set gels at the pH range near the isoelectric point (pI) of the main whey proteins, but heated gels were more deformable (did not exhibit rupture point) and showed greater elasticity modulus. However, gels formed by heating far from the pI (pH 6.7 or 3.5) showed more fragile structure, indicating that, in these mixed gels, there are prevailing biopolymers interactions. Cold-set and heat-set gels at pH near or below the WP pI showed strain-weakening behavior, but heated gels at neutral pH showed strong strain-hardening behavior. Such results suggest that differences in stress-strain curve at the nonlinear part of the data could be correlated to structure particularities obtained from different gelation processes.
dc.description4
dc.description1
dc.description23
dc.description31
dc.languageen
dc.publisherSpringer
dc.publisherNew York
dc.publisherEUA
dc.relationFood Biophysics
dc.relationFood Biophys.
dc.rightsfechado
dc.rightshttp://www.springer.com/open+access/authors+rights?SGWID=0-176704-12-683201-0
dc.sourceWeb of Science
dc.subjectWhey proteins
dc.subjectGelation process
dc.subjectHeat-set gels
dc.subjectCold-set gels
dc.subjectMechanical properties
dc.subjectBST equation
dc.subjectHeat-denatured Whey
dc.subjectCold-set Gels
dc.subjectRheological Properties
dc.subjectFunctional-properties
dc.subjectComplex Coacervation
dc.subjectBeta-lactoglobulin
dc.subjectMixed Systems
dc.subjectAcacia Gum
dc.subjectIsolate
dc.subjectPh
dc.titleWhey Protein/Arabic Gum Gels Formed by Chemical or Physical Gelation Process
dc.typeArtículos de revistas


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