Physico-chemical properties and component interactions in high solids food systems

dc.check.embargoformatNot applicableen
dc.check.infoNo embargo requireden
dc.check.opt-outNoen
dc.check.reasonNo embargo requireden
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dc.contributor.advisorKerry, Joseph P.en
dc.contributor.authorPotes, Naritchaya
dc.contributor.funderDepartment of Agriculture, Food and the Marine, Irelanden
dc.date.accessioned2014-03-31T13:29:35Z
dc.date.available2014-03-31T13:29:35Z
dc.date.issued2014
dc.date.submitted2014
dc.description.abstractThe present study aimed to investigate interactions of components in the high solids systems during storage. The systems included (i) lactose–maltodextrin (MD) with various dextrose equivalents at different mixing ratios, (ii) whey protein isolate (WPI)–oil [olive oil (OO) or sunflower oil (SO)] at 75:25 ratio, and (iii) WPI–oil– {glucose (G)–fructose (F) 1:1 syrup [70% (w/w) total solids]} at a component ratio of 45:15:40. Crystallization of lactose was delayed and increasingly inhibited with increasing MD contents and higher DE values (small molecular size or low molecular weight), although all systems showed similar glass transition temperatures at each aw. The water sorption isotherms of non-crystalline lactose and lactose–MD (0.11 to 0.76 aw) could be derived from the sum of sorbed water contents of individual amorphous components. The GAB equation was fitted to data of all non-crystalline systems. The protein–oil and protein–oil–sugar materials showed maximum protein oxidation and disulfide bonding at 2 weeks of storage at 20 and 40°C. The WPI–OO showed denaturation and preaggregation of proteins during storage at both temperatures. The presence of G–F in WPI–oil increased Tonset and Tpeak of protein aggregation, and oxidative damage of the protein during storage, especially in systems with a higher level of unsaturated fatty acids. Lipid oxidation and glycation products in the systems containing sugar promoted oxidation of proteins, increased changes in protein conformation and aggregation of proteins, and resulted in insolubility of solids or increased hydrophobicity concomitantly with hardening of structure, covalent crosslinking of proteins, and formation of stable polymerized solids, especially after storage at 40°C. We found protein hydration transitions preceding denaturation transitions in all high protein systems and also the glass transition of confined water in protein systems using dynamic mechanical analysis.en
dc.description.sponsorshipDepartment of Agriculture, Food and the Marine (Food Institutional Research Measure (FIRM) 08/R&D/TMFRC/651)en
dc.description.statusNot peer revieweden
dc.description.versionAccepted Version
dc.format.mimetypeapplication/pdfen
dc.identifier.citationPotes, N. 2014. Physico-chemical properties and component interactions in high solids food systems. PhD Thesis, University College Cork.en
dc.identifier.endpage182
dc.identifier.urihttps://hdl.handle.net/10468/1495
dc.language.isoenen
dc.publisherUniversity College Corken
dc.rights© 2014, Naritchaya Potesen
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/en
dc.subjectNonenzymatic browningen
dc.subjectHigh protein systemsen
dc.subjectProtein hydrationen
dc.subjectProtein denaturationen
dc.subjectProtein oxidationen
dc.subjectWhey proteinsen
dc.subjectLactose crystallizationen
dc.subjectAdditivity of water sorptionen
dc.subjectMolecular sizeen
dc.subjectOil reactant mediumen
dc.subjectProtein aggregationen
dc.subject.lcshLactoseen
dc.subject.lcshWheyen
dc.thesis.opt-outfalse
dc.titlePhysico-chemical properties and component interactions in high solids food systemsen
dc.typeDoctoral thesisen
dc.type.qualificationlevelDoctoralen
dc.type.qualificationnamePhD (Food Science and Technology)en
ucc.workflow.supervisorjoe.kerry@ucc.ie
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