Claim · model-written summary
Bran albumin/globulin was richer in lysine and asparagine/aspartic acid than other fractions.
- Taxon
- Wheat
Triticum aestivumt0 - Outcome
- lysine and asparagine/aspartic acide0
- Direction
- richere0
- Comparator
- other OPFe0
Not reportedMaterialGeneCompoundOrgan / stageInteractorInteractor roleSecond interactorSecond interactor roleTreatmentSettingValueQualifier
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“It is richer in lysine and asparagine/aspartic acid than other OPF.”
e1“Albumin/globulin is the most abundant OPF.”
t0“Wheat”
Title
Extractability and Chromatographic Characterization of Wheat ( Triticum aestivum L.) Bran Protein
N. De Brier; S.V. Gomand; I. Celus; et al. Journal of Food Science 2015. doi:10.1111/1750-3841.12856
Other claims from this paper (14)
- Observation Albumin/globulin was the most abundant wheat bran protein fraction.
- Observation Most bran albumin/globulin proteins were below 30 k molecular weight.
- Observation Bran albumin/globulin chromatographic profiles differed from flour profiles.
- Observation Wheat bran prolamin had high proline and glutamine/glutamic acid levels.
- Observation Bran prolamin was rich in proteins of 30 to 45 k molecular weight.
- Observation Bran prolamin also had protein around 66 k, attributed to endosperm gliadin contamination.
- Observation Bran glutelin had high glycine, proline and glutamine/glutamic acid levels.
- Observation Bran glutelin had intermediate and high molecular weight proteins, with few below 30 k.
- Observation Flour high molecular weight glutenin subunits were also present in bran.
- Observation Flour low molecular weight glutenin subunits were also present in bran.
- Intervention effect Ball milling released wheat bran albumin/globulin.
- Intervention effect Ball milling released wheat bran glutelin.
- Intervention effect Ball milling did not release wheat bran prolamin.
- Observation A substantial portion of bran glutelin was trapped in aleurone cells and was not endosperm glutenin.