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dc.contributor.authorKehoe, Joseph James
dc.contributor.authorMorris, Edwin R
dc.contributor.authorBrodkorb, Andre
dc.date.accessioned2014-01-21T15:32:10Z
dc.date.available2014-01-21T15:32:10Z
dc.date.issued22/11/2006
dc.identifier.citationKehoe, J. J., Morris, E. R., & Brodkorb, A. (2007). The influence of bovine serum albumin on [beta]-lactoglobulin denaturation, aggregation and gelation. Food Hydrocolloids, 21(5-6), 747-755. DOI: 10.1016/j.foodhyd.2006.10.001en_GB
dc.identifier.issn0268-005X
dc.identifier.urihttp://hdl.handle.net/11019/513
dc.descriptionpeer-revieweden_GB
dc.description.abstractThe effect of bovine serum albumin (BSA) on the heat-induced denaturation, aggregation and subsequent acid-induced gelation of β-lactoglobulin (β-lg) was investigated in this work. Changes in the denaturation kinetics of β-lg during heating at 78 °C were determined by monitoring the disappearance of the native protein by reverse-phase chromatography. Replacing β-lg with increasing amounts of BSA, while keeping the total protein concentration constant at 5% (w/w), significantly increased the denaturation rate of β-lg from 2.57±0.30×10−3(g L−1)(1−n)s−1 to 5.07±0.72×10−3(g L−1)(1−n)s−1 (β-lg: BSA ratio of 3:1 w/w). The reaction order for β-lg was 1.40±0.09. Partial replacement of β-lg with BSA (β-lg: BSA ratio of 3:1 w/w) significantly increased the reaction order to 1.67±0.13. Heat-induced aggregates between β-lg and BSA were studied by dynamic light scattering, two-dimensional electrophoresis and size exclusion chromatography. The partial replacement of β-lg with BSA significantly changed the gelling properties of the acid-induced gels. A rapid rate of acidification resulted in a significant decrease, while a slow acidification rate resulted in a significant increase in gel strength. Size exclusion chromatography demonstrated that intermolecular disulphide bond formation occurred during both heat-induced denaturation/aggregation and subsequent acid-induced gelation. Results clearly indicate that BSA contributed to the formation of these disulphide bonds.en_GB
dc.description.sponsorshipThis work was funded under the Food Institutional Research Measure (FIRM) of the National Development Plan 2000-2006. J. Kehoe is funded by the Teagasc Walsh Fellowship scheme
dc.language.isoenen_GB
dc.publisherElsevieren_GB
dc.relation.ispartofseriesFood Hydrocolloids;vol 21
dc.subjectβ-lactoglobulinen_GB
dc.subjectDenaturationen_GB
dc.subjectBovine Serum Albuminen_GB
dc.subjectThiol groupsen_GB
dc.subjectKineticsen_GB
dc.subjectGelationen_GB
dc.titleThe influence of bovine serum albumin on β-lactoglobulin denaturation, aggregation and gelationen_GB
dc.typeArticleen_GB
dc.identifier.rmisNFFM-0203-4764
dc.identifier.rmisMDDT-0103-5452
dc.identifier.doihttp://dx.doi.org/10.1016/j.foodhyd.2006.10.001
dc.contributor.sponsorDepartment of Agriculture, Food and the Marine
dc.contributor.sponsorTeagasc Walsh Fellowship Programme
refterms.dateFOA2018-01-12T07:55:01Z


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