Gel chromatography of sunflower proteins

Sabir, Mohammad A.; Sosulski, F. W.; MacKenzie, S. L.

doi:10.1021/jf60190a036

Cited by 41 publications

(38 citation statements)

References 11 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Several authors have claimed that, in sunflower products, CGA appears mainly in the form of complexes or bound to proteins. The binding to sunflower proteins has been reported to occur either preferentially with low‐molecular‐weight proteins48–52 or high‐molecular‐weight proteins53 or non‐preferentially 54, 55. Non‐covalent interactions of both caffeic and quinic acids (constituents of CGA) with helianthinin have also been reported 56.…”

Section: Phenolic Compounds Of Sunflower Seedmentioning

confidence: 99%

Sunflower proteins: overview of their physicochemical, structural and functional properties

2007

View full text Add to dashboard Cite

There is increasing worldwide demand for proteins of both animal and plant origin. However, animal proteins are expensive in terms of both market price and environmental impact. Among alternative plant proteins, sunflower seeds are particularly interesting in view of their widespread availability in areas where soy is not or only sparsely produced. Compared with other sources of vegetable proteins, sunflower seeds have been reported to have a low content of antinutritional factors. Although the absence of these factors is important, the functionality of the protein preparations will mainly determine their applicability. This review provides detailed information about sunflower seed composition and processing, including processes to remove phenolic compounds from meals. The main part of the review concerns the structure and functionality of the two major protein fractions, helianthinin and 2S albumins. Regarding functionality, emphasis is on solubility, thermal behaviour and surface activity. Protein structure and functionality are discussed as a function of extrinsic factors such as pH, ionic strength, temperature and the presence of other seed components, particularly chlorogenic acid. In addition, sunflower proteins are compared from a structural and functional point of view with other plant proteins, particularly soy proteins.

show abstract

Section: Phenolic Compounds Of Sunflower Seedmentioning

confidence: 99%

Sunflower proteins: overview of their physicochemical, structural and functional properties

2007

View full text Add to dashboard Cite

show abstract

“…The major storage proteins in bean seeds are summarized as follows: (1) albumins (2S fraction; 20% to 30% of total proteins, soluble in water) consisting of two dimers (PA1, 11 kDa and PA2, 25 kDa) and tetramer (lectin, 50 kDa) and (2) globulins (50% to 75% of total proteins, soluble in salt) containing vicilin (7S fraction; a 50-kDa trimer), legumin (11S fraction; α acid and ß basic polypeptides of 40 and 20 kDa, respectively, bound by a disulfide bridge), and convicilin (a 71-kDa trimer) [24,25]. In the present investigation, we examine the impact of copper excess on bean seed germination, embryonic growth, and changes in the cotyledonary biomass mobilization, particularly, the breakdown of albumin and globulin.…”

Section: Introductionmentioning

confidence: 99%

Copper Excess Impairs Mobilization of Storage Proteins in Bean Cotyledons

Karmous¹,

Ferjani²,

Chaoui³

2011

Biol Trace Elem Res

View full text Add to dashboard Cite

Germination represents a limiting stage of plant life cycle. One of the underlying metabolic activities following imbibition of seed is the reserve mobilization. Seeds of bean (Phaseolus vulgaris L. var. soisson nain hatif) were germinated by soaking in distilled water or 200 μM CuCl(2). Storage proteins breakdown and amino acids freeing from reserve tissues were investigated. Compared to the control, Cu caused a reduction in germination rate, embryo growth, and in mobilization of cotyledonary biomass. The failure in albumin and globulin hydrolysis after the exposure to the pollutant was argued by (1) higher contents of remaining proteins than control ones, (2) persistence of some polypeptide bands resolved by polyacrylamide gel electrophoresis of albumin and globulin-rich fractions, and (3) decrease in the availability of amino acids. Nitrogen starvation in embryonic axis should be associated with the Cu-imposed delay in growth.

show abstract

“…Rahma and Rao (1979) observed that while there are many reports on the processing and technological aspects of sunflower oil and meal, data on characterization of proteins are meager. This was also confirmed by Sabir et al, 1973;Baudet and Mosse, 1977). Rahma and Rao conducted a study to determine the characterization of the proteins of sunflower cultivated in India.…”

Section: Sulfur 1943mentioning

confidence: 71%