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Rapeseed storage proteins

The major rapeseed storage proteins are a 12S type globulin, called cruciferin, which makes up 60% of the total protein, and a 2S type albumin, called napin, which makes up 20% of the total protein [9, 10]. Both of these proteins are formed in embryonic cells and stored in specialized vacuoles known as protein bodies. [Pg.41]

Fig. 3.2 Rapeseeds were germinated from 12to 168 h in airlift tank. The total soluble proteins were extracted and separated by 15% SDS-PAGE. The gel was stained with Coomassie blue. Between 36 and 60 h, the degradation of storage proteins and the de novo synthesis of Rubisco is clearly visible. Fig. 3.2 Rapeseeds were germinated from 12to 168 h in airlift tank. The total soluble proteins were extracted and separated by 15% SDS-PAGE. The gel was stained with Coomassie blue. Between 36 and 60 h, the degradation of storage proteins and the de novo synthesis of Rubisco is clearly visible.
Murphy, D.J., Cummins, I. and Kang, A.S. (1989) Synthesis of the major oil-body membrane protein in developing rapeseed (Brassica napus) embryos. Integration with storage-lipid and storage-protein synthesis and implications for the mechanism of oil-body formation. Biochem. J. 258, 285-293. [Pg.87]

WHY IS RAPESEED PROTEIN EXTRACTION MORE DIFFICULT 10.3.1 Storage Proteins... [Pg.189]

Rapeseed contains two major storage proteins the 2 S albumin napin with a molar weight of 12-17 kDa and the 12 S globulin cruciferin with a molar weight of about 300 kDa. The napin cruciferin ratio depends on the rapeseed variety and is for canola-type quality about 1.1-1.3. This is significantly different to soyabean, which contains about 90% globulin (Schwenke, 1994 Natsch, 2006). [Pg.189]

Since the rapeseed contains two different major storage proteins with quite different properties and some specific secondary plant substances which react with the proteins under certain conditions, rapeseed protein extraction becomes difficult. Each single processing step influences resulting protein yield and quality. Therefore, the process design strongly depends on the targeted application of the extracted proteins. [Pg.201]

There are a large number of oilseeds some of them are very important because they yield edible oils. Among them are soybean (Glycine max), rapeseed (Brassica campestris), coconut (Cocos nucifera), and sunflower (Helianthus annuus). In addition to their lipid content, ranging from 20 to 55%, oilseeds often have substantial amounts of protein stored as protein bodies (30% or more v/v) and saccharides stored as cell wall components. Thus, the main subcellular structure consists of protein bodies 5 to 20 pm in diameter, surrounded by a cytoplasmic protein network in which are embedded the oil storage sites (Figure 2.1). These lipid bodies, sometimes referred to as spherosomes, are only 0.2 to 0.5 pm in diameter and are connected through a thin envelope. [Pg.19]

Very recently, a distinct but similar class of oleosin-like proteins also containing the characteristic central hydrophobic domain has been found in the pollen of rapeseed and corresponding genes have been isolated from both rapeseed and Arabidopsis [1]. Like seeds, pollen cells are propagules which carry their own storage compounds which are required to support their metabolism after germination. In the case of rapeseed and Arabidopsis, Ae seeds and pollen each contain oil bodies and are desiccation tolerant [Ij. This established a correlation between desiccation tolerance and the presence of oil body proteins in both gametophytic and sporophytic plant tissues. [Pg.558]


See other pages where Rapeseed storage proteins is mentioned: [Pg.341]    [Pg.98]    [Pg.64]    [Pg.77]    [Pg.77]    [Pg.588]    [Pg.62]    [Pg.361]    [Pg.53]    [Pg.283]    [Pg.588]    [Pg.321]    [Pg.140]    [Pg.458]   
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