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The emulsifying properties of three genetic variants of β -lactoglobulin ( β -lac) (the A, B and C variants) are investigated as a function of protein concentration. Differences in the emulsifying properties and emulsion stability are explained in view of the known differences in physico-chemical and structural/conformational properties of the β -lac variants. β -lac A forms the finest emulsion droplets, and β -lac C the largest droplets. The order of decreasing emulsifying ability (A>B>C) can be explained in terms of differences in the molecular structure, and conformational stability of the variant proteins. The creaming stability, when compared at the same particle size, is greatest for β -lac C, with β -lac A and B having a similar and lower stability. The differences in creaming stability may arise from a higher surface coverage for the β -lac C droplets at an equivalent particle size. The storage stability is lower for β -lac A than for β -lac B and C, which both show a similar behaviour. Storage stability differences are discussed in terms of differences in molecular structure, conformational stability, interfacial viscosity and surface coverage for the three variants. |
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