Zur Rheologie und Verspinnung alkalischer Lösungen aus Ackerbohnenprotein und Casein

Schmandke, H.; Paul, D. A. L.; Gensrich, H.‐J.; Friebe, R.; Anger, H.; Luther, H.; Bartsch, DK; Maune, R.

doi:10.1002/food.19760200512

Cited by 18 publications

(3 citation statements)

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“…The material under research are fibers of Vicia fuba protein-casein (1 : l), prepared according to [2] (diameter 40-80 pm, dry matter 37-41 per cent, pH value 2.5-3.0).…”

Section: Methodsmentioning

confidence: 99%

Changes in the chemical and functional properties of protein fibers by reaction with carbonyl compounds. Part II. Reaction of arginine and amido groups. Quantitative determination of reacting carbonyl groups

Schmandke

Hartmann

1979

Nahrung

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The arginine content of Viciu fabu protein/casein(l: 1)-fibers is made to decrease up to 50 per cent by reaction with glyoxal and up to 15 per cent by dialdehyde starch. Formaldehyde and glutaric dialdehyde do not influence the arginine content. The content in amido groups is not affected by the reaction with glyoxal, dialdehyde starch, formaldehyde, and glutaric dialdehyde. The reaction of the fiber protein with the quoted aldehydes increases in the following order: glyoxal < formaldehyde < dialdehyde starch < glutaric dialdehyde and is dependent on the concentration of the specific aldehyde.In part I [l] the blocking of lysine in the reaction of protein fibers with carbonyl compounds and the changes in the functional property ,,shear strength" have been reported. Part II deals with the participation of arginine and amido groups in the reaction. Moreover, the reaction of fiber protein with carbonyl compounds is determined quantitatively. Material and methodsThe material under research are fibers of Vicia fuba protein-casein (1 : l), prepared according to [2] (diameter 40-80 pm, dry matter 37-41 per cent, pH value 2.5-3.0).The following aldehydes have been used: formaldehyde 30%, glyoxal 40%, glutaric dialdehyde 25 %, and dialdehyde starch (degree of oxidation about loo%), prepared by oxidation of starch with periodic acid at pH 4 according to MEHLTRE~ER [3].The treatment of protein fibers with aldehydes has been carried out at pH 6, according to part I [I]. Arginine has been determined by colour reaction, according to SAKAGUCHI, by reaction with alpha-naphtho1 and hypobromite [5]. At first the sample is to partially hydrolyse for 6 h in 6 N hydrochloric acid (ratio protein:hydrochloric acid = 1 : 1000). In order to separate by-products which may interfere with the reaction, the hydrolysate is purified by column chromatography (length of column: 15 cm, diameter: 0.9 cm, cation exchange resin: Amberlite 1R 120, eluting solvent: sodium citrate buffer pH 4.25 and 5.28 according to MOORE et a].[6], speed of elution: 30 ml/hr.). The determination of arginine in the eluate (buffer 5.28) has been carried out according to IZUMI [4, 51. The calculation of the arginine content was enabled by an external standard for each series.Dedicated to the 60th birthday of Prof. Dr. H. HAENEL Part I Nahrung 21, 215 (1977)

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“…The material under research are fibers of Vicia fuba protein-casein (1 : l), prepared according to [2] (diameter 40-80 pm, dry matter 37-41 per cent, pH value 2.5-3.0).…”

Section: Methodsmentioning

confidence: 99%

Changes in the chemical and functional properties of protein fibers by reaction with carbonyl compounds. Part II. Reaction of arginine and amido groups. Quantitative determination of reacting carbonyl groups

Schmandke

Hartmann

1979

Nahrung

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“…1.5%, NaCl cone. 15%) [7], DAS-CVF (aldehyde cone. 10 mg/g protein) was prepared by treatment of the protein fibers with a DAS solution (cone.…”

Section: Dietsmentioning

confidence: 99%

Effect of Spinning and Additional Cross-Linking with Dialdehyde Starch or Aluminum Ions on the Digestibility and Quality of Casein-<i>Vicia faba</i>Protein Isolate Mixtures

et al. 1985

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Studies were made in adult rats using an isotopic ¹⁵N method. Whole egg, wheat, casein and Viciafaba protein isolate served as reference proteins. The diets were isonitrogenous and feed intake was adjusted to the maintenance energy level. Variations in true N digestibility were small (91.8–96.1%). The amount of metabolic fecal nitrogen in animals receiving the diet containing wheat was 9.4 mg/l00 g body weight compared with 4.9–5.8 mg in the other diets. The differences in nutritional quality for maintenance between proteins of plant and animal origin were small. However, spinning (alkaline treatment) and additional cross-linking with aluminum ions or dialdehyde starch affected the nutritional quality for maintenance.

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“…Amongst the various sources of vegetable proteins studied for possible human consumption, Vicia Faba seed has interesting nutritional and technological properties. The preparation of protein isolates (Flink and Christiansen 1973;Petit et al 1975;Olsen 1978), the nutritional value (Pion et al 1975) and the texturization by cookingextrusion (De La Gueriviere et al 1978) or by spinning (Schmandke et al 1976) of Fababean protein have been studied.…”

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Spinning of Fababean Protein 1. Flow Properties of Fababean Protein Dopes by Capillary Extrusion Viscometry

Culioli¹,

Sale²

1981

Journal of Texture Studies

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Flow properties of Fababean protein dopes were studied by capillary extrusion viscometry. The consistency of these dopes was time dependent for pH values between 11 and 13 and it increased slightly with time. At still higher pH values it decreased sharply after 1 h aging. For protein concentration between 11% and 15% (w/w), and pH 11–13.5, these dopes exhibited shear thinning behaviour in the shear rate range 500–20,000 s−1 and they followed the power law τ= cγn. This relationship could be written in the dimensionally homogeneous form: When the protein concentration of the dopes increased the power law index (n) decreased and the consistency index (C) increased. A maximum consistency was reached at pH 12.5 while the power law index was minimum. The results can be explained in terms of protein‐protein interactions and of macromolecule denaturation.

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Zur Rheologie und Verspinnung alkalischer Lösungen aus Ackerbohnenprotein und Casein

Cited by 18 publications

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Changes in the chemical and functional properties of protein fibers by reaction with carbonyl compounds. Part II. Reaction of arginine and amido groups. Quantitative determination of reacting carbonyl groups

Changes in the chemical and functional properties of protein fibers by reaction with carbonyl compounds. Part II. Reaction of arginine and amido groups. Quantitative determination of reacting carbonyl groups

Effect of Spinning and Additional Cross-Linking with Dialdehyde Starch or Aluminum Ions on the Digestibility and Quality of Casein-<i>Vicia faba</i>Protein Isolate Mixtures

Spinning of Fababean Protein 1. Flow Properties of Fababean Protein Dopes by Capillary Extrusion Viscometry

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