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 453343
Title The potential of aqueous fractionation of lupin seeds for high-protein foods
Author(s) Berghout, J.A.M.; Boom, R.M.; Goot, A.J. van der
Source Food Chemistry 159 (2014). - ISSN 0308-8146 - p. 64 - 70.
DOI https://doi.org/10.1016/j.foodchem.2014.02.166
Department(s) Food Process Engineering
VLAG
Publication type Refereed Article in a scientific journal
Publication year 2014
Keyword(s) functional-properties - isoelectric precipitation - rheological properties - thermal-damage - albus - angustifolius - ultrafiltration - sustainability - isolate - sweet
Abstract Aqueous fractionation of protein from lupin seeds was investigated as an alternative to the conventional wet fractionation processes, which make use of organic solvents. The effect of extraction temperature was studied and the consequences for downstream processing were analysed. Omitting the extraction of oil with organic solvents resulted in a protein isolate that contained 0.02–0.07 g oil g-1 protein isolate, depending on the exact extraction conditions. Nevertheless, the protein functionality of the aqueous fractionated lupin protein isolate was similar to the conventional lupin protein isolate. The protein isolate suspension could be concentrated to 0.25 g mL-1 using ultrafiltration, which provides a relevant concentration for a range of high-protein products. Based on the results, we conclude that aqueous fractionation can be a method to lower the environmental impact of the extraction of proteins from legumes that contain water- and dilute salt-soluble proteins.
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