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SAXS and other spectroscopic analysis of 12S cruciferin isolated from the seeds of Brassica nigra
Journal of Molecular Structure, 2017Abstract Oilseeds of the plant family Brassicaceae are important for providing both lipid and protein contents to human nutrition. Cruciferins (12S globulins) are seed storage proteins, which are getting attention due to their allergenic and pathogenicity related nature.
Khaliq, Binish +9 more
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International Journal of Biological Macromolecules
Plant protein emulsifiers, particularly rapeseed protein isolate with its superior amino acid composition and predominantly globular protein, have captured significant interest in the food industry. Nonetheless, the application of these proteins has been stymied by their lackluster emulsification properties.
Shengqing, Hu +5 more
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Plant protein emulsifiers, particularly rapeseed protein isolate with its superior amino acid composition and predominantly globular protein, have captured significant interest in the food industry. Nonetheless, the application of these proteins has been stymied by their lackluster emulsification properties.
Shengqing, Hu +5 more
openaire +2 more sources
Plant Science, 1990
Abstract Cruciferin (12S globulin) is a large, neutral, oligomeric protein synthesized in rapeseed (Brassica napus) during seed development. It is composed of six subunit pairs. Each pair is synthesized as a precursor which in turn gives rise to one heavy α chain ( M r approx. 30 000) and one light β chain ( M r approx.
Joakim Rödin, Lars Rask
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Abstract Cruciferin (12S globulin) is a large, neutral, oligomeric protein synthesized in rapeseed (Brassica napus) during seed development. It is composed of six subunit pairs. Each pair is synthesized as a precursor which in turn gives rise to one heavy α chain ( M r approx. 30 000) and one light β chain ( M r approx.
Joakim Rödin, Lars Rask
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Theoretical and Applied Genetics, 1995
The levels of certain essential amino acids, in particular cysteine, lysine and methionine, in the seed storage protein of a commercial spring variety of rape, Brassica napus, have been increased by the introduction of an antisense gene for cruciferin, which is the most abundant storage protein in rapeseed. The antisense construct contained part of the
J, Kohno-Murase +3 more
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The levels of certain essential amino acids, in particular cysteine, lysine and methionine, in the seed storage protein of a commercial spring variety of rape, Brassica napus, have been increased by the introduction of an antisense gene for cruciferin, which is the most abundant storage protein in rapeseed. The antisense construct contained part of the
J, Kohno-Murase +3 more
openaire +2 more sources
Food Biophysics, 2013
The influence of pH (3.0, 5.0, and 7.0) and ionic strength (0, 50, 100 mM NaCl) on the physicochemical and emulsifying properties of a cruciferin-rich protein isolate (CPI) was investigated. Surface charge on the CPI was found to substantially reduced in the presence of NaCl.
Lamlam Cheung +2 more
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The influence of pH (3.0, 5.0, and 7.0) and ionic strength (0, 50, 100 mM NaCl) on the physicochemical and emulsifying properties of a cruciferin-rich protein isolate (CPI) was investigated. Surface charge on the CPI was found to substantially reduced in the presence of NaCl.
Lamlam Cheung +2 more
openaire +1 more source