Transition from Fractal to Spherical Aggregates of Globular Proteins: Brownian-Like Activation and/or Hydrodynamic Stress?

Author(s): Najet Mahmoudi, Cedric Gaillard, Alain Riaublanc, Francois Boue, Monique A.V. Axelos.

Journal Name: Current Topics in Medicinal Chemistry

Volume 14 , Issue 5 , 2014

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We report on the structure of whey protein aggregates formed by a short heating coupled to shear at high temperatures (80-120) and neutral pH in scale-up processing conditions, using gel filtration chromatography, light scattering, small angle neutron scattering, and cryogenic transmission electron microscopy. The results are interpreted in terms of coexistence of residual non-aggregated proteins and aggregates. The characteristics of aggregates such as the size, the aggregation number and the shape evidence two different morphologies. Whereas aggregates formed at 80 °C show a selfsimilar structure down to a length scale of the monomer with a fractal dimension typical for reaction limited cluster aggregation (D~2.2), aggregates formed at higher temperature show a spherical morphology, with the structure from small angle neutron scattering data best modelled with the form factor of a polydisperse sphere. We compare the structure of these aggregates to that of aggregates formed in quiescent conditions at lab scale. The structure transition is interpreted in terms of a non-trivial interplay between three perturbation factors: interparticle interaction, temperature and shear.

Keywords: Whey globular protein, aggregation, structure, small angle neutron scattering, light scattering, cryogenic transmission electron microscopy.

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Article Details

Year: 2014
Page: [630 - 639]
Pages: 10
DOI: 10.2174/1568026614666140118211906
Price: $58

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