Isolation and partial characterization of flaxseed (Linum usitatissimum L.) proteins

Dev, D. K.; Sienkiewicz, T.; Quensel, E.; Hansen, R.

doi:10.1002/food.19860300350

Cited by 10 publications

(1 citation statement)

References 6 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…length x diameter) using 0.5 "6 SDS -0.05 M Tris-glycine (pH 8.3) buffer system [2]. The relative intensity of the stained bands on polyacrylamide gel was determined by scanning the cylindrical gels with a Hitachi dual wavelength chromatoscanner.…”

Section: Methodsmentioning

confidence: 99%

Isolation and subunit composition of 11 S globulin of linseed (Linum usitatissimum L.)

Dev

Sienkiewicz²

1987

Nahrung

Self Cite

View full text Add to dashboard Cite

Early reports on linseed proteins are mostly concerned with solubilization of total proteins from oil-free meal by different solvents and their isolation [6, 81, paper electrophoretic characterization and amino acid composition [7]. Classification of proteins in defatted linseed meal, based on their solubilities in various solvents, has shown the salt-soluble protein to be a major fraction in linseed [3, 91. Employing different physicochemical techniques, it has been demonstrated that total proteins of linseed consist of at least 3 components of which the major one, apparently, is a high molecular weight globulin [Z, 41. MADHUSUDHAN et al. [5] isolated the major fraction of linseed proteins and reported its physicochemical characteristics. Here, we report the isolation of linseed globulin by a different procedure and its characterization by sodium dodecyl sulphate -polyacrylamide gel electrophoresis (SDS-PAGE) and sedimentation analysis. Material and methodsSeeds, purchased locally, were milled and defatted by repeated extractions, alternately, with diethyl ether and acetone at 4 C . Total proteins were extracted from the oil-free meal, following desolventization at room temperature and passing through a 0.25 mm screen, with phosphate buffer containing I .O M NaCl using meal :solvent ratio of 1 : 20. The clear extract, obtained by repeated centrifugations (3000 x g for I5 min) at 20 C, was diluted with 5.5 times its volume ofdistilled water and kept at 4 'C for several hours. The cryoprecipitated globulin was separated by centrifuging at 4 C and dissolved in a small volume of the extractant. The process of precipitation and centrifugation was repeated twice. Finally, the isolated protein was dissolved in the extractant buffer to which sodium azide was added at a concentration of 0.02"/,. This sample was called "crude globulin".The crude globulin fraction was eluted through a Sephadex (3-200 column using phosphate buffer as described elsewhere (21. The ultraviolet absorption spectrum of the eluate at 280 nm showed a peak with a prominent shoulder. The eluate fraction corresponding to the peak were pooled. concentrated by ultrafiltration using a PM-10 membrane with a cut-off limit of 10000 daltons and rechromatographed to obtain a somewhat symmetric peak. The eluate volume under this peak was diluted in the ratio 3 : 5 with distilled water and concentrated 10-fold by ultrafiltration using the same membrane. This was referred to as "purified globulin".Electrophoresis was carried out on 8.79< polyacrylamide disc gels ( 5 x 0.5 cm. length x diameter) using 0.5 "6 SDS -0.05 M Tris-glycine (pH 8.3) buffer system [2]. The relative intensity of the stained bands on polyacrylamide gel was determined by scanning the cylindrical gels with a Hitachi dual wavelength chromatoscanner. Peak areas were determined by integration from the densitometric scans of the PAGE gels and the relative proportions of the major subunits were calculated.The sedimentation coefficient (s;,,,) of purified globulin was determined according to BEHL...

show abstract

Section: Methodsmentioning

confidence: 99%

Isolation and subunit composition of 11 S globulin of linseed (Linum usitatissimum L.)

Dev

Sienkiewicz²

1987

Nahrung

Self Cite

View full text Add to dashboard Cite

show abstract

Flaxseed as a functional food source

2001

View full text Add to dashboard Cite

Flaxseed is emerging as one of the key sources of phytochemicals in the functional food arena. In addition to being one of the richest sources of a-linolenic acid oil and lignans,¯axseed is an essential source of high-quality protein and soluble ®bre and has considerable potential as a source of phenolic compounds. The implications of diets containing¯axseed or its components for human nutrition and disease prevention are analysed in this paper. Results of the ®rst meta-analysis examining the relationship between intake of¯axseed or its components and risk reduction of disease in humans is presented. Some areas of potential opportunities and impact of using¯axseed or its components in the diet are highlighted.

show abstract

Linum Species (Flax): In Vivo and in Vitro Accumulation of Lignans and Other Metabolites

Uden

Pras

Woerdenbag

1994

Medicinal and Aromatic Plants VI

View full text Add to dashboard Cite

Isolation and partial characterization of flaxseed (Linum usitatissimum L.) proteins

Cited by 10 publications

References 6 publications

Isolation and subunit composition of 11 S globulin of linseed (Linum usitatissimum L.)

Isolation and subunit composition of 11 S globulin of linseed (Linum usitatissimum L.)

Flaxseed as a functional food source

Linum Species (Flax): In Vivo and in Vitro Accumulation of Lignans and Other Metabolites

Contact Info

Product

Resources

About