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

Nutritional Components of Amaranth Seeds and Vegetables: A Review on Composition, Properties, and Uses

“…A relationship was also supposed between these 2 species and A. lividus , and between A. powellis and A. deflexus , which by their electrophoretic patterns were assigned to the same biotype (Zheleznov and others ). The studies of physicochemical properties of 11S globulin (one of the most important and abundant storage proteins of the amaranth seed) suggested that the cumulative effects of many factors are responsible for its high thermal stability, whereas the balance between surface hydrophobicity and hydrophilicity is important for good emulsifying property (Tandang‐Silvas and others ).…”

“…Significantly softer crumb texture of pseudocereal‐containing breads was characterized by an effect that was attributed to the presence of natural emulsifiers in the pseudocereal flours. Recently, it was shown that one of the most abundant and important storage proteins of the amaranth grain, 11S globulin, possesses good emulsifying property (Tandang‐Silvas and others ), which might have a positive effect on dough formation.…”

Proteins of Amaranth (Amaranthus spp.), Buckwheat (Fagopyrum spp.), and Quinoa (Chenopodium spp.): A Food Science and Technology Perspective

“…The literature often refers to this fraction as “albumin‐2,” “minor albumin,” or “globulin‐P.” However, even if these proteins are extracted with water, salt is present in the flour as a result of the 1st extraction with salt solution. These proteins are thus most likely globulins, especially because they share several features with other amaranth globulins such as molecular size and surface reactivity (Drzewiecki and others ; Aphalo and others ; Quiroga and others ; Tandang‐Silvas and others ). Already at low salt concentrations (≤0.01 M), the structure of the so‐called albumin‐2 evolves into a partially unfolded conformation, which may trigger aggregate formation (Castellani and others ).…”

“…The proglobulin is subsequently transported to the protein storage vacuoles. Herein, its post‐translational cleavage by an endopeptidase releases acidic and basic chains and triggers the assembly of 2 trimers into a homohexamer (Tandang‐Silvas and others ; Carrazco‐Pena and others ). This homohexamer is made up of subunits with MMs between 52 and 59 kDa, each consisting of an acidic (34 to 36 kDa, pI 5.6) and a basic (22 to 24 kDa, pI 9.2) protein linked by an SS‐bond (Konishi and others ; Barba de la Rosa and others ; Barba de la Rosa and others ; Valdez‐Ortiz and others ).…”

“…Near‐UV (240 to 320 nm) CD intensities revealed that the purified 7S globulin secondary structure is relatively poor in α‐helices, but possesses high levels of β‐sheets (Marcone ). The secondary structure of the amaranth globulins has been estimated to consist of 31% α‐helices, 27% β‐sheets, and 42% aperiodic structure (Drzewiecki and others ), while that of the albumin‐2 fraction, which most likely also contains globulins, has been estimated as 16% α‐helices, 41% β‐sheets, and 53% aperiodic structure (Tandang‐Silvas and others ) and less hydrophobic surfaces than the albumins, as follows from 8‐anilinonaphthalene‐1‐sulfonic acid fluorescence measurements (Gorinstein and others ).…”