Conservation and divergence on plant seed 11S globulins based on crystal structures

Tandang‐Silvas, Mary Rose; Fukuda, Tomoko; Fukuda, Chisato; Prak, Krisna; Cabanos, Cerrone; Kimura, Aiko; Itoh, Takafumi; Mikami, Bunzo; Utsumi, Shigeru; Maruyama, Nobuyuki

doi:10.1016/j.bbapap.2010.02.016

Cited by 99 publications

(128 citation statements)

References 41 publications

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“…Although there is a small difference in the ionic strength used for T m measurement, the T m values obtained from amaranth 11S proglobulin are relatively high compared with the other 11S proglobulins (350.0-368.0 K) (Maruyama, Maruyama, Mikami, & Utsumi, 2004;Tandang-Silvas et al, 2010b). The stabilizing effect of NaCl on 11S seed globulins has been corroborated by the other studies on rapeseed (Tandang, Adachi, Inui, Maruyama, & Utsumi, 2004), soybean, pea and faba bean (Kimura et al, 2008;Maruyama et al, 1999).…”

Section: Structural Factors and Thermal Stabilitymentioning

confidence: 55%

Crystal structure of a major seed storage protein, 11S proglobulin, from Amaranthus hypochondriacus: Insight into its physico-chemical properties

et al. 2012

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Section: Structural Factors and Thermal Stabilitymentioning

confidence: 55%

Crystal structure of a major seed storage protein, 11S proglobulin, from Amaranthus hypochondriacus: Insight into its physico-chemical properties

et al. 2012

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“…Approximately 80-90% of proteins in mature seeds are composed of a few groups of storage proteins massively accumulated in discrete vesicles, which serve as source of amino acids for germination and early growth of seedlings (Chua et al, 2008). Saline-soluble storage globulins are the main protein fraction of several seeds and constitute about 50-90% of the total protein content in legumes, 70-80% in some cereals as oats and rice and 40-90% in oilseeds as sunflower (González-Pérez & Vereijken, 2007;Shewry & Halford, 2002;Tandang-Silvas et al, 2010). Based on their sedimentation coefficients, globulins are classified into two groups: 7S or vicilins and 11S or legumins (Shewry et al, 1995;Tandang-Silvas, Tecson-Mendoza, Mikami, Utsumi, & Maruyama, 2011).…”

Section: Introductionmentioning

confidence: 99%

Purification and biochemical characterization of 11S globulin from chan (Hyptis suaveolens L. Poit) seeds

Bojórquez‐Velázquez

Lino-López²,

Huerta‐Ocampo

et al. 2016

Food Chemistry

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“…Structural organization of cruciferin up to quaternary level has been described (Adachi et al, 2003;Dalgalarrondo et al, 1986;Plietz et al, 1983;Tandang-Silvas et al, 2010). The mature cruciferin contains six subunits or protomers that assemble as two trimer units in which each protomer is comprised of two polypeptide; α-(∼40 kDa, 254 to 296 amino acids and β-(∼20 kDa, 189 to 191 amino acids) chain linked via a disulfide bond (Adachi et al, 2003;Dalgalarrondo et al, 1986;Tandang-Silvas et al, 2010).…”

Section: Cruciferinmentioning

confidence: 99%

Canola/rapeseed protein-functionality and nutrition

Wanasundara¹,

McIntosh²,

Perera³

et al. 2016

OCL

136

103

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-Protein rich meal is a valuable co-product of canola/rapeseed oil extraction. Seed storage proteins that include cruciferin (11S) and napin (2S) dominate the protein complement of canola while oleosins, lipid transfer proteins and other minor proteins of non-storage nature are also found. Although oil-free canola meal contains 36-40% protein on a dry weight basis, non-protein components including fibre, polymeric phenolics, phytates and sinapine, etc. of the seed coat and cellular components make protein less suitable for food use. Separation of canola protein from non-protein components is a technical challenge but necessary to obtain full nutritional and functional potential of protein. Process conditions of raw material and protein preparation are critical of nutritional and functional value of the final protein product. The storage proteins of canola can satisfy many nutritional and functional requirements for food applications. Protein macromolecules of canola also provide functionalities required in applications beyond edible uses; there exists substantial potential as a source of plant protein and a renewable biopolymer. Available information at present is mostly based on the protein products that can be obtained as mixtures of storage protein types and other chemical constituents of the seed; therefore, full potential of canola storage proteins is yet to be revealed.Keywords: Canola / rapeseed storage proteins / cruciferin / napin / protein digestibility / functional properties Résumé -Protéines de canola et de colza : fonctionnalités et nutrition. Les tourteaux riches en protéines repré-sentent un coproduit de valeur de l'extraction de l'huile de canola/colza. Dans la graine, les protéines de stockage, notamment la cruciférine (11S) et la napine (2S), dominent la fraction protéique du canola, mais des oléosines, des protéines de transfert de lipides et d'autres protéines mineures non dédiées au stockage sont également présentes. Bien que le tourteau de canola déshuilé contienne 36-40 % de protéines sur poids sec, la présence de composants non protéiques, dont les fibres, les polymères phénoliques, les phytates, la sinapine, etc. issus de l'enveloppe de la graine et des composants cellulaires rendent les protéines moins appropriées à une utilisation en alimentation humaine. Cette revue présente les connaissances actuelles en termes de valeur nutritionnelle et fonctionnelle des protéines issues des graines de canola. La séparation des protéines de canola des composants non protéiques représente un défi technique mais nécessaire pour libérer totalement le potentiel nutritionnel et fonctionnel de la protéine. Les protéines de stockage de canola peuvent satisfaire un grand nombre d'exigences nutritionnelles et fonctionnelles pour des applications alimentaires. Les macromolécules protéiques de canola offrent également des fonctionnalités requises dans les applications dépassant les seules utilisations alimentaires ; un potentiel important existe en tant que source de protéines végétales et de biopol...

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Conservation and divergence on plant seed 11S globulins based on crystal structures

Cited by 99 publications

References 41 publications

Crystal structure of a major seed storage protein, 11S proglobulin, from Amaranthus hypochondriacus: Insight into its physico-chemical properties

Crystal structure of a major seed storage protein, 11S proglobulin, from Amaranthus hypochondriacus: Insight into its physico-chemical properties

Purification and biochemical characterization of 11S globulin from chan (Hyptis suaveolens L. Poit) seeds

Canola/rapeseed protein-functionality and nutrition

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