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dc.contributor.authorCucheval, Aurelie Suzanne Bernadette
dc.date.accessioned2010-03-28T22:58:20Z
dc.date.availableNO_RESTRICTIONen_US
dc.date.available2010-03-28T22:58:20Z
dc.date.issued2009
dc.identifier.urihttp://hdl.handle.net/10179/1209
dc.description.abstractFirstly, the effect of pectin on acid milk gels in concentrated, quiescent systems was investigated by passive microrheology using two complementary techniques: diffusive wave spectroscopy (DWS) and multiple particle tracking (MPT). DWS, by allowing probing the mechanical properties of the network at high frequency, gave information on its microstructure. The addition of high methoxyl pectins was shown to change the network structure which has been explained by bridging of the casein micelles by the polymer as the system was undergoing acidification. On the other hand, the presence of low methoxyl pectin in the acid milk gel was shown to have no effect on the microstructure of the network at low concentration of polymer (0.1%w/w) which has been attributed to the sensitivity of this low DM pectin to calcium: LM pectin are trapped by calcium and not able to interact with casein micelles anymore. Multiple particle tracking was used to probe the effect of pectin on the heterogeneity of the system by following the distribution of the displacements of added micro beads at a given time lag during the gelation using the Van Hove distribution. Furthermore, the surface chemistry of the probes was modified in an attempt to control their location in the system. Finally, the mean square displacements of the casein micelles obtained by DWS and, of k-casein coated particles obtained by MPT were shown to give good agreement for the same acid milk system. Having established that the interaction between casein micelles and low methoxyl pectin is prevented by the pectin sensitivity to calcium, the effect of the pectin fine structure was investigated on the interaction between k-casein and pectin by surface plasmon resonance (SPR). The amount of pectin binding on a k-casein coated gold surface was shown to be strongly dependant on the pectin fine structure. It was concluded that small negative patches on the pectin backbone, likely to comprise of around two consecutive unmethylesterified galacturonic acid, are the most effective for pectin binding to k-casein. The effect of the direct interaction between pectin and k- casein on ‘calcium-free casein micelle mimics’ in pectin solution was then investigated using coated latex beads. A pectin structure with a limited number of negative patches on its backbone was also shown to limit the potential for destabilization via bridging.en_US
dc.language.isoenen_US
dc.publisherMassey Universityen_US
dc.rightsThe Authoren_US
dc.subjectAcid milk gelsen_US
dc.subjectPectin-casein interactionen_US
dc.subject.otherFields of Research::240000 Physical Sciences::249900 Other Physical Sciences::249901 Biophysicsen_US
dc.titleInvestigations of the behaviour of pectin in casein micelle systems and their analogues : thesis presented for the degree of Doctor of Philosophy in Physicsen_US
dc.typeThesisen_US
thesis.degree.disciplinePhysicsen_US
thesis.degree.grantorMassey Universityen_US
thesis.degree.levelDoctoralen_US
thesis.degree.levelDoctoralen
thesis.degree.nameDoctor of Philosphy (Ph.D.)en_US


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