Structure of the rapeseed 1.7 S storage protein, napin, and its precursor.

Ericson, Mats; Rödin, Joakim; Lenman, Marit; Glimelius, Kristina; Josefsson, Lars; Rask, Lars

doi:10.1016/s0021-9258(18)66909-1

Cited by 149 publications

(28 citation statements)

References 27 publications

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“…Characterization of these strongly basic proteins found them to be composed of two polypeptides, approximately 90 and 30 amino acids in length, respectively, linked by disulfide bridges with a total molecular mass of 12–14 kDa [ 132 ]. Subsequent experiments demonstrated that both napin chains were generated from the cleavage of a common precursor polypeptide [ 133 ].…”

Section: Seed Storage Proteins Of the Brassicaceae Familymentioning

confidence: 99%

Breeding Canola (Brassica napus L.) for Protein in Feed and Food

Duncan

2021

Plants

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Interest in canola (Brassica napus L.) In response to this interest, scientists have been tasked with altering and optimizing the protein production chain to ensure canola proteins are safe for consumption and economical to produce. Specifically, the role of plant breeders in developing suitable varieties with the necessary protein profiles is crucial to this interdisciplinary endeavour. In this article, we aim to provide an overarching review of the canola protein chain from the perspective of a plant breeder, spanning from the genetic regulation of seed storage proteins in the crop to advancements of novel breeding technologies and their application in improving protein quality in canola. A review on the current uses of canola meal in animal husbandry is presented to underscore potential limitations for the consumption of canola meal in mammals. General discussions on the allergenic potential of canola proteins and the regulation of novel food products are provided to highlight some of the challenges that will be encountered on the road to commercialization and general acceptance of canola protein as a dietary protein source.

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Section: Seed Storage Proteins Of the Brassicaceae Familymentioning

confidence: 99%

Breeding Canola (Brassica napus L.) for Protein in Feed and Food

Duncan

2021

Plants

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“…In oilseed rape plants this protein is named as napins. Ericson et al [51] suggested that the napins consist of two polypeptide chains with M, values of −9000 and 4000, linked together with interchain disulfide bonds. The synthesis of napins gave rise a single precursor proteins in which proteolytic cleavage occurred.…”

Section: Albuminsmentioning

confidence: 99%

“…The synthesis of napins gave rise a single precursor proteins in which proteolytic cleavage occurred. Due to this cleavage the loss of a linker peptide and short peptides from both the N and C termini was reported [51,52]. All the 2 s albumins are compact globular proteins with conserved cysteine residues inspite of differing in their subunit structure and synthesis.…”

Section: Albuminsmentioning

confidence: 99%

Impact of Inadequate Concentration of Boron in Seed Storage Proteins Content in Oilseed Crops

Archana¹,

Verma²,

Pandey³

2021

Grain and Seed Proteins Functionality

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For the estimation of Impact of inadequate concentration of boron in seed storage proteins content in oilseed crops, a sand culture experiment was designed and all the three crops i.e. soyabean, mustard and linseed were grown under sufficient and insufficient boron treatment till maturity. Seed germination and seed storage protein concentration was determined in seeds after the harvesting of crops. Earlier oilseed crops like soyabean, mustard and linseed are cultivated for oil production but at this time these crops are reliable source of protein also and are real asset for human dietary protein. The storage protein present in seeds varies from ~10% (in cereals) to 40% (in certain legumes and oilseeds) of dry weight. Seeds contain one or more groups of proteins that are present in high amounts and that serve to provide a store of amino acids and sulfur required during germination and seedling growth. Quality of seeds is driven by the total protein content present in the form of storage reserve in seeds. There are major four types of storage proteins known as- globulins (insoluble in water), albumins (soluble in water), prolamins (soluble in alcohol) and glutelins (soluble in dilute acid and alkaline medium). Globulins and albumins are the major storage seed proteins of legumes and oilseed crops whereas prolamins and glutelins are mostly found in cereal seeds. Functionally boron is crucial micronutrient for a considerable amount of agricultural yield. Seed reserves (proteins, carbohydrates, starch, lipids) of post harvested seeds are depended on the appropriate boron supply during cropping. Boron insufficiency in oilseed crops found to be an inhibitory factor for seed vigor and seed quality. So this chapter deals with the effect of boron deprivation on seed quality in terms of germination capacity and seed storage protein reserves in the post harvested seeds of soybean, mustard and linseed.

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“…The seeds of many diverse plant species, including Brazil nut (Ampe et al, 1986;Sun et al, 1987a), rapeseed (Crouch et al, 1983;Ericson et al, 1986), cotton (Galau et al, 1992), sunflower (Kortt et al, 1991), castor bean (Sharief and Li, 1982), Lupine (Gayler et al, 1990), Arabidopsis (Krebbers et al, 1988), faba bean (Pasqualini et al, 1991), and amaranth (Segura-Nieto et al, 1992), contain 2S proteins, a class of low molecular mass (about 12 kDa) proteins. These proteins are water-soluble albumins and are abundant in the seeds, as 20-60% of the total seed protein (Yule and Huang, 1981).…”

Section: Introductionmentioning

confidence: 99%

Purification and Characterization of the Methionine-Rich 2S Seed Proteins from the Brazil Nut Family (Lecythidaceae)

Zuo

Sun

1996

J. Agric. Food Chem.

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2S seed proteins were purified from paradise nut (Lecythis zabucajo) and cannonball (Couroupita quianensis), two members of the Brazil nut family (Lecythidaceae). The amino acid composition, subunit structure, partial protein sequence, immunoreactivity, and processing pattern of these proteins were determined. The 2S proteins from both paradise nut (PN2S) and cannonball (CB2S) are rich in the sulfur amino acids, especially methionine (Met): 14.0% Met and 4.3% cysteine (Cys) in PN2S; 19.9% Met and 4.5% Cys in CB2S. Both 2S proteins are synthesized as a precursor polypeptide of 18 kDa and processed stepwise to form the 9- and 3-kDa mature subunit polypeptides. These properties are similar to those of the Brazil nut (Bertholletia excelsa H.K.B.) 2S protein (BN2S). However, while the 18-kDa precursor polypeptide of PN2S, like that of BN2S, undergoes three sequential cleavages to form the two mature subunits, only two stepwise cleavages occur during the processing of CB2S. Keywords: Met-rich protein; 2S protein; seed proteins; Brazil nut

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Structure of the rapeseed 1.7 S storage protein, napin, and its precursor.

Cited by 149 publications

References 27 publications

Breeding Canola (Brassica napus L.) for Protein in Feed and Food

Breeding Canola (Brassica napus L.) for Protein in Feed and Food

Impact of Inadequate Concentration of Boron in Seed Storage Proteins Content in Oilseed Crops

Purification and Characterization of the Methionine-Rich 2S Seed Proteins from the Brazil Nut Family (Lecythidaceae)

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