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dc.contributor.authorLoveday, SM
dc.contributor.authorWang, X. L.
dc.contributor.authorRao, M. A.
dc.contributor.authorAnema, S. G.
dc.contributor.authorSingh, Harjinder
dc.date.accessioned2011-11-09T22:14:10Z
dc.date.accessioned2016-03-06T22:26:44Z
dc.date.available2011-11-09T22:14:10Z
dc.date.available2016-03-06T22:26:44Z
dc.date.issued2012-05
dc.identifier.citationLoveday, S. M., Wang, X. L., Rao, M. A., Anema, S. G., & Singh, H. β-Lactoglobulin nanofibrils: Effect of temperature on fibril formation kinetics, fibril morphology and the rheological properties of fibril dispersions. Food Hydrocolloids, 27(1), 242-249en_US
dc.identifier.issn0268005X
dc.descriptionAuthor manuscripten_US
dc.descriptionNOTICE: this is the author’s version of a work that was accepted for publication in Food Hydrocolloids. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Food Hydrocolloids, 27(1),(2012) DOI: 10.1016/j.foodhyd.2011.07.001
dc.description.abstractAlmost all published studies of heat-induced β-lactoglobulin self-assembly into amyloid-like fibrils at low pH and low ionic strength have involved heating at 80°C, and the effect of heating temperature on self-assembly has received little attention. Here we heated β-lactoglobulin at pH 2 and 75°C, 80°C, 90°C, 100°C, 110°C or 120°C and investigated the kinetics of self-assembly (using Thioflavin T fluorescence), the morphology of fibrils, and the rheological properties of fibril dispersions. Self-assembly occurred at all temperatures tested. Thioflavin T fluorescence increased sigmoidally at all temperatures, however it decreased sharply with >3.3 h heating at 110°C and with >5 h heating at 120°C. The sharp decreases were attributed partly to local gelation, but destruction of fibrils may have occurred at 120°C. Thioflavin T fluorescence results indicated that maximal rates of fibril formation increased with increasing temperature, especially above 100°C, but fibril yield (maximum Thioflavin T fluorescence) was not affected by temperature. At 100ºC and 110ºC, fibrils were slightly shorter than at 80°C, but otherwise they looked very similar. Fibrils made by heating at 120°C for 1 h were also similar, but heating at 120°C for 8 h gave predominantly short fibrils, apparently the products of larger fibrils fragmenting. Heating at 100°C gave consistently higher viscosity than at 80°C, and heating for >2 h at 120°C decreased viscosity, which may have been linked with fibril fragmentation seen in micrographs.en_US
dc.language.isoenen_US
dc.publisherElsevieren_US
dc.subjectβ-Lactoglobulinen_US
dc.subjectWhey proteinsen_US
dc.subjectMilken_US
dc.subjectHeaten_US
dc.subjectSelf-assemblyen_US
dc.subjectProteinsen_US
dc.subjectAmyloiden_US
dc.subjectFibrilsen_US
dc.subjectDenaturationen_US
dc.subjectAciden_US
dc.subjectBeta-lactoglobulin
dc.titleβ-Lactoglobulin nanofibrils: Effect of temperature on fibril formation kinetics, fibril morphology and the rheological properties of fibril dispersionsen_US
dc.typeArticleen_US
dc.rights.holderCopyright: Elsevier
dc.identifier.elements-id176254
dc.identifier.harvestedMassey_Dark
dc.identifier.harvestedMassey_Dark


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