Benjamin O, Silcock P, Beauchamp J, Büttner A, Everett DW (2014)
Publication Type: Journal article
Publication year: 2014
Publisher: Wiley-Blackwell
Book Volume: 79
Pages Range: E2014-E2022
The emulsifying properties of plant legume protein isolates (soy, pea, and lupin) were compared to a milk whey protein, β-lactoglobulin (β-lg), and a nonionic surfactant (Tween 20). The protein fractional composition was characterized using sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis. The following emulsion properties were measured: particle diameter, shear surface ζ-potential, interfacial tension (IT), and creaming velocity. The effect of protein preheat treatment (90 °C for 10 min) on the emulsifying behavior and the release of selected volatile organic compounds (VOCs) from emulsions under oral conditions was also investigated in real time using proton transfer reaction-mass spectrometry. The legume proteins showed comparable results to β-lg and Tween 20, forming stable, negatively charged emulsions with particle diameter d
APA:
Benjamin, O., Silcock, P., Beauchamp, J., Büttner, A., & Everett, D.W. (2014). Emulsifying properties of legume proteins compared to beta-lactoglobulin and Tween 20 and the volatile release from oil-in-water emulsions. Journal of Food Science, 79, E2014-E2022. https://doi.org/10.1111/1750-3841.12593
MLA:
Benjamin, Ofir, et al. "Emulsifying properties of legume proteins compared to beta-lactoglobulin and Tween 20 and the volatile release from oil-in-water emulsions." Journal of Food Science 79 (2014): E2014-E2022.
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