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.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 559924
Title Microfluidic investigation of the coalescence susceptibility of pea protein-stabilised emulsions: Effect of protein oxidation level
Author(s) Hinderink, E.B.A.; Kaade, Wael; Sagis, L.M.C.; Schroen, C.G.P.H.; Berton-Carabin, C.C.
Source Food Hydrocolloids 102 (2020). - ISSN 0268-005X - 10 p.
DOI https://doi.org/10.1016/j.foodhyd.2019.105610
Department(s) Food Process Engineering
VLAG
Physics and Physical Chemistry of Foods
Publication type Refereed Article in a scientific journal
Publication year 2020
Keyword(s) Plant proteins - Emulsion stability - Emulsification - langmuir-blodgett-films
Abstract Proteins are used to stabilise oil-in-water (O/W) emulsions, and plant proteins are gaining interest as functional ingredients due to their higher sustainability potential compared to e.g., dairy proteins. However, their emulsifying properties are not that well understood, and depend on how their production process affects their physicochemical status. In the present work, we use the soluble fraction of commercial pea protein isolate to stabilise O/W emulsion droplets formed in a microfluidic device, and record coalescence stability after droplet formation (11–173 ms) for different protein concentrations (0.1–1 g/L). For the shortest adsorption times (11–65 ms) droplets were unstable, whereas for longer adsorption times differences in coalescence stability could be charted. Metal-catalysed oxidation of pea proteins performed for up to 24-h, prior to emulsion formation and analysis, increased the coalescence stability of the droplets, compared to fresh pea proteins. This may be explained by oxidation-induced protein fragmentation, leading to low molecular weight products. The Langmuir-Blodgett films looked highly heterogeneous for films prepared with fresh or mildly oxidised (3-h) proteins, and was more homogenous for 24-h oxidised proteins. This could be the cause for the observed differences in emulsion coalescence stability, structurally heterogeneous films being more prone to rupture. From this work, it is clear that the emulsifying properties of pea are strongly dependent on their chemical status, and associated structural properties at the molecular and supramolecular levels. The present microfluidic device is an efficient tool to capture such effects, at time scales that are relevant to industrial emulsification.
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