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Please use this identifier to cite or link to this item: http://hdl.handle.net/11019/513

Title: The influence of bovine serum albumin on β-lactoglobulin denaturation, aggregation and gelation
Authors: Kehoe, Joseph James
Morris, Edwin R
Brodkorb, Andre
Keywords: β-lactoglobulin
Bovine Serum Albumin
Thiol groups
Issue Date: 22-Nov-2006
Publisher: Elsevier
Citation: Kehoe, 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.2006.10.001
Series/Report no.: Food Hydrocolloids;vol 21
Abstract: The 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.
Description: peer-reviewed
This 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
URI: http://hdl.handle.net/11019/513
ISSN: 0268-005X
Appears in Collections:Food Chemistry & Technology

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