rapeseed/albumin

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Behaviors of bovine serum albumin and rapeseed proteins at the air/water interface after grafting aliphatic or aromatic chains.

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The influence of grafting aliphatic or aromatic groups on the behaviors of bovine serum albumin (BSA) and rapeseed proteins (napin and cruciferin) at the air/water interface is studied. From compression isotherms, it is shown that the chemical modification induces an increase in the interfacial

Behaviour of a protein isolate from rapeseed (Brassica napus) and its main protein components - globulin and albumin - at air/solution and solid interfaces, and in emulsions.

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The behaviour of a rapeseed protein isolate (RI) and its main protein components - globulin (RG) and albumin (RA) - in adsorbed and spread monolayers, as well as in emulsions was investigated. Tensiometry, film-pressure area and Langmuir-Blodgett-techniques, and emulsion parameters were used to

Structural analysis of the small chain of the 2S albumin, napin nIII, from rapeseed. Chemical and spectroscopic evidence of an intramolecular bond formation.

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Napin nIII is a 2S albumin from rapeseed (Brassica napus L.) homologous to the major mustard allergen. It is composed of two different polypeptide chains linked by two disulphide bonds. The small chain has been isolated by reverse-phase HPLC after reduction of the native protein and its primary

A new distinct group of 2 S albumins from rapeseed. Amino acid sequence of two low molecular weight napins.

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Two napins (nIa and nIb), isolated from Brassica napus (rapeseed) seeds, have been sequenced. The two proteins show the common structural pattern of the 2 S albumins, since they are composed of two disulfide-linked chains of different size, yet they exhibit an atypical low molecular weight (12.5 kDa

A new size-exclusion chromatography method for fast rapeseed albumin and globulin quantification.

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The method described in the article aims at the quantification of both main storage proteins, globulins and albumins, in aqueous extract from rapeseed, as an alternative to the current reference methods, Kjeldahl and SDS-PAGE electrophoresis. The new method lies on the analytical separation of

Solution structure and stability against digestion of rproBnIb, a recombinant 2S albumin from rapeseed: relationship to its allergenic properties.

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NMR spectroscopy has been used to determine the solution structure of the precursor form of the recombinant napin BnIb, rproBnIb, a 2S albumin, 109-residue protein from the seeds of Brassica napus. More than 90% of the side-chain proton resonances were unambiguously assigned from the analysis of

[Seed proteins. 3. Isolation and characterization of albumin of sunflowers and rapeseed].

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[Spinning of rapeseed proteins].

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Alkaline solutions of a mixture from rapeseed globulin and casein show plastic flow, which is influenced by protein concentration, relation of rapeseed globulin and casein, temperature and time of storage of the protein solution. The sodium hydroxide concentration with a great variability doesn't

Alcalase rapeseed inhibitors: purification and partial characterization.

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Extensive rapeseed protein hydrolysate obtained sequentially with Alcalase and Flavourzyme showed inhibitory activity towards Alcalase. Inhibitory activity decreased as the hydrolytic process progressed probably by heat denaturation and/or partial protease degradation. Alcalase rapeseed inhibitors

Influence of the rapeseed protein hydrolysis process on CHO cell growth.

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Different protein hydrolysates were prepared from enzymatic hydrolyses of a rapeseed isolate (>90% protein content) using different commercial enzymes of non-animal origin. The extent of hydrolysis was controlled to produce hydrolysates corresponding to various degrees of hydrolysis (DH) from 5 to

Effect of Diet Supplemented With Rapeseed Meal or Hydrolysable Tannins on the Growth, Nutrition, and Intestinal Microbiota in Grass Carp (Ctenopharyngodon idellus).

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Grass carp (Ctenopharyngodon idellus; n = 320) were received four different diets for 56 days. The experimental diets were: fishmeal (FM) containing 10% fishmeal (without rapeseed meal), and rapeseed meal (RM) containing 50% rapeseed meal (without fishmeal), and two semi-purified diets

Toxicological evaluation of rapeseed products in a subacute feeding study in rats.

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Groups of 15 male rats were fed ad libitum for 4 weeks standard diet containing 0, 2.5, 5 or 10% rapeseed protein isolate (RPI), 2.5, 5 or 10% rapeseed extraction residue (RER) or 10% casein. Body weight gain and food intake were recorded weekly. Clinical chemistry analyses, haematology, urinalysis,

Binding of erucic acid with human serum albumin using a spectroscopic and molecular docking study.

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Erucic acid (EA) is one of the key fatty acids usually found in canola oil, mustard oil and rapeseed oil. Consumption of EA in primates was found to cause myocardial lipidosis and cardiac steatosis. To have an insight of the effect of EA in humans, we performed in vitro interaction studies of EA

Emulsifying properties of acylated rapeseed (Brassica napus L.) peptides.

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A peptide fraction having an average size of 5.6 amino acids has been purified from a rapeseed hydrolyzate, acylated using C(10)-C(14) acyl chlorides, and the surface tension values at the air-water interface and emulsifying properties studied. As compared with standard surface-active proteins, such

Recombinant pronapin precursor produced in Pichia pastoris displays structural and immunologic equivalent properties to its mature product isolated from rapeseed.

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2S albumin storage proteins from rapeseed (Brassica napus), called napins, consist of two different polypeptide chains linked by disulphide bridges, which are derived by proteolytic cleavage from a single precursor. The precursor form of the napin BnIb (proBnIb) has been cloned using a PCR strategy

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