Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

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Record number 424404
Title Surface rheology of interfaces stabilized by different structures of BSA
Author(s) Arsianti, Y.A.; Baptist, H.G.M.; Linden, E. van der; Sagis, L.M.C.
Event ISFRS 2012, Zürich, 2012-04-10/2012-04-13
Department(s) Physics and Physical Chemistry of Foods
Publication type Poster (professional)
Publication year 2012
Abstract The interfacial rheology of three different structures of bovine serum albumin (BSA), i.e. BSA fibrils, soluble BSA pectin complexes, and native BSA, were investigated. At a bulk concentration of 0.05 %(w/w), there is only a small difference in the equilibrium surface tension of O/W interfaces stabilized with these three structures. However, there is a significant difference in the dilatational elastic and viscous modulus at low strain, which becomes less pronounced at high strain. Interfaces stabilized by BSA pectin complexes show the highest dilatational elastic and viscous modulus, followed by those stabilized by BSA fibrils and native BSA, for all strains measured (0.005 - 0.40). Frequency sweeps show that in the applied range of frequencies (0.005 - 0.1 1/s), the response of interfaces stabilized by complexes is significantly different from the response of interfaces stabilized by monomer and fibrils. The loss tangent of the former is considerably higher and decreases with increasing frequency, whereas the latter two display a loss tangent that is almost constant (~ 0.2) in the applied range of frequencies. The interfacial shear rheology of interfaces O/W interfaces stabilized by complexes, fibrils and native monomers is measured as a function of bulk concentration. For all concentrations (0.002 - 0.2 %(w/w)), the elastic and viscous modulus of interfaces stabilized by complexes is the highest, followed by fibrils and monomer. The elastic and viscous modulus of BSA fibrils and monomers increase as a function of concentration, up to a concentration of 0.2 %(w/w). However, the elastic and viscous modulus of the complex reaches a plateau at a concentration of 0.03 %(w/w), which suggest that at this point the interface is already saturated. This study has shown that O/W interfaces stabilized by BSA fibrils and BSA pectin soluble complexes have a surface rheology remarkably different from interfaces stabilized by native BSA. These aggregation states of BSA may find application as emulsifiers or foam stabilizers
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