Comparative Studies of Subunit Compositions of Legumins from Various Cultivars of<i>Vicia faba</i>L. Seeds

Utsumi, Shigeru; Yokoyama, Zen-ichi; Mori, Tomohiko

doi:10.1080/00021369.1980.10863994

Cited by 7 publications

(4 citation statements)

References 11 publications

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“…Among the genotypes, legumin accounted for 35 to 62% of the quantified peak area while vicilin/convicilin for 20–34% (Figure ). These results are comparable with the findings of Utsumi, Yokoyama, and Mori who reported ranges of 42 to 47% and 28 to 31% for 11 and 7S globulins in crude protein extracts of six Vf cultivars analyzed by the sucrose density gradient fractionation technique. In another study, the Vf legumin and vicilin content reportedly varied between 40 to 45% and 20 to 25%, respectively .…”

Section: Results and Discussionsupporting

confidence: 91%

“…However, given the underlying genetic complexity of these broadly defined classes of storage proteins, concrete exploitation of genetic variation in seed protein composition for the development of cultivars with improved protein profiles would require identification of the genes encoding the major seed storage proteins, as well as understanding their synthesis, transport, and storage mechanisms. To date, studies have referred to just a few major protein subunits of legumin and vicilin ,,− and although Liu et al identified several additional nonglobulin seed storage proteins from Vf by mass spectrometry, the identification of the full set of proteins that contribute to the nutritional and functional properties of the Vf seed is far from complete.…”

Section: Introductionmentioning

confidence: 99%

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Identification and Quantification of Major Faba Bean Seed Proteins

Warsame

Michael

O’Sullivan

et al. 2020

J. Agric. Food Chem.

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Faba bean ( Vicia faba L. ) holds great importance for human and animal nutrition for its high protein content. However, better understanding of its seed protein composition is required in order to develop cultivars that meet market demands for plant proteins with specific quality attributes. In this study, we screened 35 diverse Vicia faba genotypes by employing the one-dimensional sodium dodecyl sulfate–polyacrylamide gel electrophoresis (1D SDS-PAGE) method, and 35 major protein bands obtained from three genotypes with contrasting seed protein profiles were further analyzed by mass spectrometry (MS). Twenty-five of these protein bands (MW range: ∼ 9–107 kDa) had significant (p ≤ 0.05) matches to polypeptides in protein databases. MS analysis showed that most of the analyzed protein bands contained more than one protein type and, in total, over 100 proteins were identified. These included major seed storage proteins such as legumin, vicilin, and convicilin, as well as other protein classes like lipoxygenase, heat shock proteins, sucrose-binding proteins, albumin, and defensin. Furthermore, seed protein extracts were separated by size-exclusion high-performance liquid chromatography (SE-HPLC), and percentages of the major protein classes were determined. On average, legumin and vicilin/convicilin accounted for 50 and 27% of the total protein extract, respectively. However, the proportions of these proteins varied considerably among genotypes, with the ratio of legumin:vicilin/convicilin ranging from 1:1 to 1:3. In addition, there was a significant (p < 0.01) negative correlation between the contents of these major fractions (r = −0.83). This study significantly extends the number of identified Vicia faba seed proteins and reveals new qualitative and quantitative variation in seed protein composition, filling a significant gap in the literature. Moreover, the germplasm and screening methods presented here are expected to contribute in selecting varieties with improved protein content and quality.

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Section: Results and Discussionsupporting

confidence: 91%

Section: Introductionmentioning

confidence: 99%

Identification and Quantification of Major Faba Bean Seed Proteins

Warsame

Michael

O’Sullivan

et al. 2020

J. Agric. Food Chem.

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“…The seed storage proteins of legumes contain legumin that occurs in large amounts and appears to be made up of twelve subunits, of which six subunits are acidic and six subunits are basic in nature (Derbyshire et al, 1976). The diversity of the subunit composition of legumin among cultivars has been shown by Harada (1972) and Kitamura et al (1980) for soybean, by Tombs (1965) for groundnut, by Blagrove and Gillespie (1978) for lupin, by Thomson and Schroeder (1978) and Casey (1979) for pea, and by Utsumi et al (1980) for broad bean. We have recently demonstrated that the subunit compositions of glycinins isolated from the seeds of various cultivars of soybean vary among the cultivars and may he classified into five groups according to differing molecular charges of the subunits (Mori et al, 1981).…”

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confidence: 99%

Cultivar differences in gelling characteristics of soybean glycinin

Nakamura¹,

Utsumi²,

Kitamura³

et al. 1984

J. Agric. Food Chem.

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“…4 ) The subunit compositions of legumins of these cultivars differ among themselves with respect to the molecular charges of their subunits. 5 ) We have also observed such heterogeneity in glycinin, a legumin-like protein, obtained from various soybean cultivars. 6 ) In the present study, we analyzed the legumin as follows: the molecular species were separated by polyacrylamide gel electrophoresis, and then the composition of their subunits was analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis.…”

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confidence: 83%