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Rapeseed Protein Isolate as a Sustainable Alternative to Soy Protein: A Case Study on Chicken Pâtés. [PDF]

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Ikonić P   +7 more
europepmc   +1 more source

Studies on Structure-Physicochemical Function Relationships of Soybean β-Conglycinin and Rapeseed Cruciferin

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The cruciferin gene family in radish

Plant Molecular Biology, 1992
In order to analyse the cruciferin gene family in radish a cDNA library was screened either with heterologous rapeseed probes or by differential screening and sequencing. We could identify six partial cDNA clones belonging to two different groups of cruciferin genes which do not cross-hybridize, and probably three distinct subfamilies.
Depigny-This, D.   +4 more
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Structural and Physicochemical Property Relationships of Cruciferin Homohexamers

Journal of Agricultural and Food Chemistry, 2013
Heteromeric cruciferin from wild type (WT) Arabidopsis thaliana and homomeric cruciferin CRUA, CRUB, and CRUC composed of identical subunits obtained from double-knockout mutant lines were investigated for their structural and physicochemical properties.
Thushan S, Withana-Gamage   +4 more
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Characterization of a Brassica napus gene encoding a cruciferin subunit: estimation of sizes of cruciferin gene families

Plant Molecular Biology, 1992
A gene encoding a subunit of the 12S storage globulin, cruciferin, in Brassica napus (oilseed rape) has been isolated and characterized. The gene consists of about 2200 bp including three short intervening sequences. Primer extension analysis showed that the major transcription start site is located 30 bp 5' of the predicted ATG start codon.
J, Rödin   +3 more
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The behaviour of rapeseed cruciferin on chromatofocusing

Food / Nahrung, 1993
AbstractCruciferin, a main storage protein of rapeseeds has been investigated by means of chromatofocusing, isoelectric focusing and electrophoresis in polyacrylamide gels. It was shown, that the half molecules of this oligomeric protein differ from each other by subunit composition. There are specific forms of cruciferin.
V. A. Reva, M. T. Kulibali
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