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Solubility of a cruciferin‐rich protein product purified from rapeseed pressed cake ( Brassica napus L.) by an aqueous processing method
Author(s) -
Rehder Alina,
Sulewska Anna Maria,
Markedal Keld Ejdrup,
Sørensen Susanne,
Sørensen Jens Christian
Publication year - 2017
Publication title -
international journal of food science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.831
H-Index - 96
eISSN - 1365-2621
pISSN - 0950-5423
DOI - 10.1111/ijfs.13446
Subject(s) - rapeseed , brassica , solubility , chemistry , food science , plant protein , pea protein , aqueous solution , chromatography , by product , thaumatin , phosphate , biochemistry , biology , botany , organic chemistry , gene
Summary Pressed cake from rapeseed ( Brassica napus L.) is a promising plant protein source not yet utilised for human consumption due to the presence of antinutrients such as glucosinolates. Protein solubility is a crucial parameter influencing the functionality and thereby the applicability of proteins as food ingredients. A novel cruciferin‐rich rapeseed protein product was produced by an aqueous processing method in pilot plant scale. Intact glucosinolates were conserved by this procedure and largely removed from the protein products. Protein solubility in this product was examined when dispersed in 50 m m phosphate buffer, pH 8.0 with varying NaCl concentration (0–500 m m ). Unexpectedly, a salting‐out effect was observed of the globulin proteins, as 15.9 ± 0.6% protein was in solution at 500 m m added NaCl, whereas 21.5 ± 1.1% was solubilised without added NaCl; whether the observed effects originates from lipid and fibre constituents in the product remains to be resolved.