β-Lactoglobulin nanofibrils: Effect of temperature on fibril formation kinetics, fibril morphology and the rheological properties of fibril dispersions

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dc.contributor.authorLoveday SM
dc.contributor.authorWang XL
dc.contributor.authorRao MA
dc.contributor.authorAnema SG
dc.contributor.authorSingh H
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.descriptionAuthor manuscript
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 b-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 b-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 100 C and 110 C, 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.
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), 242-249
dc.identifier.elements-id176254
dc.identifier.harvestedMassey_Dark
dc.identifier.harvestedMassey_Dark
dc.identifier.issn0268005X
dc.identifier.urihttps://hdl.handle.net/10179/2854
dc.language.isoen
dc.publisherElsevier Ltd
dc.rights.holderCopyright: Elsevier
dc.subjectβ-Lactoglobulin
dc.subjectWhey proteins
dc.subjectMilk
dc.subjectHeat
dc.subjectSelf-assembly
dc.subjectProteins
dc.subjectAmyloid
dc.subjectFibrils
dc.subjectDenaturation
dc.subjectAcid
dc.subjectBeta-lactoglobulin
dc.titleβ-Lactoglobulin nanofibrils: Effect of temperature on fibril formation kinetics, fibril morphology and the rheological properties of fibril dispersions
dc.typeJournal article
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