Modifizierung der funktionellen Eigenschaften von Ackerbohnenprotein durch Acetylierung

Schmandke, H.; Maune, R.; Schmidt, Gert; Schultz, M.; Proll, J.

doi:10.1002/food.19770211007

Cited by 31 publications

(5 citation statements)

References 20 publications

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“…One of the most effective methods of chemical modification of proteins is the acetylation of protein amino groups 1. 2 It has been used to efficiently improve the solubility, tensioactive (emulsifying and foaming) and gelling properties of proteins from soybeans,3–5 sunflower seeds,6 peas,7 faba beans,8–10 rapeseeds11 and chickpeas12 and of other plant proteins.…”

Section: Introductionmentioning

confidence: 99%

Acetylation of faba bean legumin: conformational changes and aggregation

Schwenke¹,

Knopfe²,

Seifert

et al. 2000

J. Sci. Food Agric.

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The effect of progressive acetylation upon the conformation of the 11S globulin legumin from faba bean has been studied using chemical analysis, UV, fluorescence and CD spectroscopy, viscometry and analytical ultracentrifugation. The modification did not induce complete dissociation of the oligomeric protein. Only 30% of the protein was found to be a dissociated 3S subunit after excessive acetylation, whereas 70% was a dimeric legumin aggregate with a molecular mass of about 700 kDa. The aggregation of the highly modified legumin in high‐ionic‐strength buffer solution leads to soluble higher legumin oligomers. The acetylation resulted in a moderate molecular expansion of legumin due to a changed tertiary structure, whereas the far‐UV circular dichroism spectra did not provide definitive evidence of a decrease in domain‐stabilizing β‐sheet conformations in their secondary structure. © 2000 Society of Chemical Industry

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Section: Introductionmentioning

confidence: 99%

Acetylation of faba bean legumin: conformational changes and aggregation

Schwenke¹,

Knopfe²,

Seifert

et al. 2000

J. Sci. Food Agric.

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“…After 20 h at 22 °C followed the isolation of the insol uble acetylated protein fraction (VI) by centrifugation and of the soluble acetylated protein fraction (VIII) by precipitation at pH 4.0 in the supernatant and centrif ugation: in both cases this was followed by neutraliza tion with 0.1 N sodium hydroxide and freeze-drying. The same procedure without using acetic anhydride is valid for the preparation of the nonacetylated insolu ble (V) and soluble Vicia faba protein fraction (VII), omitting the isoelectric precipitation at pH 5.0 for the protein fraction VII [14],…”

Section: Dietsmentioning

confidence: 99%

Digestibility and Dietary Quality of Nonacetylated and Acetylated <i>Vicia faba </i>Proteins in Maintenance

et al. 1984

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N digestibility and the dietary quality of a Vicia faba protein isolate as well as of two protein fractions from this isolate, acetylated and nonacetylated, were estimated in ¹⁵N-labelled adult rats. For reference, whole egg, casein and wheat were studied. The diets were fed at maintenance energy intake level. Daily metabolic fecal nitrogen estimated by an isotopic method was 5 mg/l00 g body weight in animals receiving whole egg, casein, or Vicia faba proteins. When wheat was included in the diet metabolic fecal nitrogen was increased to 140% of this value. True N digestibility of reference proteins was 91-92% and of Vicia faba proteins 95-97%. Protein quality for maintenance was high and similar for all proteins. Acetylation affected neither N digestibility nor protein quality under maintenance conditions.

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“…Acetylation has been shown to have a beneficial effect on the functional properties of faba bean globulin 10–13…”

Section: Introductionmentioning

confidence: 99%