dc.creatorPicone, CSF
dc.creatorTakeuchi, KP
dc.creatorCunha, RL
dc.date2011
dc.dateMAR
dc.date2014-07-30T17:49:35Z
dc.date2015-11-26T16:31:44Z
dc.date2014-07-30T17:49:35Z
dc.date2015-11-26T16:31:44Z
dc.date.accessioned2018-03-28T23:12:54Z
dc.date.available2018-03-28T23:12:54Z
dc.identifierFood Biophysics. Springer, v. 6, n. 1, n. 77, n. 83, 2011.
dc.identifier1557-1858
dc.identifierWOS:000287130400009
dc.identifier10.1007/s11483-010-9177-9
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/68191
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/68191
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1270296
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionThe effects of pH (6.7 or 5.8), protein concentration and the heat treatment conditions (70 or 90 A degrees C) on the physical properties of heat-induced milk protein gels were studied using uniaxial compression, scanning electron microscopy, differential scanning calorimetry, and water-holding capacity measurements. The systems were formed from whey protein isolate (10-15% w/v) with (5% w/v) or without the addition of caseinate. The reduction in pH from 6.7 to 5.8 increased the denaturation temperature of the whey proteins, which directly affected the gel structure and mechanical properties. Due to this increase in the denaturation temperature of the beta-lactoglobulin and alpha-lactalbumin, a heat treatment of 70 A degrees C/30 min did not provide sufficient protein unfolding to form self-supporting gels. However, the presence of 5% (w/v) sodium caseinate decreased the whey protein thermo stability and was essential for the formation of self-supporting gels at pH 6.7 with heat treatment at 70 A degrees C/30 min. The gels formed at pH 6.7 showed a fine-stranded structure, with great rigidity and deformability as compared to those formed at pH 5.8. The latter had a particulate structure and exuded water, which did not occur with the gels formed at pH 6.7. The addition of sodium caseinate led to less porous networks with increased gel deformability and strength but decreased water exudation. The same tendencies were observed with increasing whey protein concentration.
dc.description6
dc.description1
dc.description77
dc.description83
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionFAPESP [2003/08119-5]
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 protein
dc.subjectSodium caseinate
dc.subjectMicrostructure
dc.subjectMechanical properties
dc.subjectpH
dc.subjectProtein denaturation
dc.subjectBeta-lactoglobulin Gels
dc.subjectThermal-denaturation
dc.subjectAlpha-lactalbumin
dc.subjectParticulate Gels
dc.subjectGelation
dc.subjectAggregation
dc.subjectMicroscopy
dc.subjectMixtures
dc.titleHeat-Induced Whey Protein Gels: Effects of pH and the Addition of Sodium Caseinate
dc.typeArtículos de revistas


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