Über Samenproteine. 3. Mitt. Isolierung und Charakterisierung der Albumine aus Sonnenblumen‐ und Rapssamen

Schwenke, K. D.; Raab, B.; Uhlig, J.; Tkocz, H.; Behlke, Joachim; Böttger, Michael; Freimuth, U.

doi:10.1002/food.19730170804

Cited by 48 publications

(15 citation statements)

References 11 publications

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“…Napin is composed of two polypeptide chains with molecular weights of 9 and 4 kDa, linked by disulfide D105, page 5 of 9 bonds. Cruciferin is consisted of 6 subunits and each subunit contains smaller units (polypeptide chains) with molecular weights in the range of 18.5 to 31.2 kDa, linked by disulfide bonds (Schwenke et al, 1973;Schwenke et al, 1983;Mieth et al, 1983;Schwenke, 1990). Based on the SDS-PAGE assay the both storage proteins were observed in the produced protein product concerning the detected bands with molecular weights of 31-29, 24-21 kDa for cruciferin polypeptide chains and 9-4 kDa for napin polypeptide chains.…”

Section: Protein Profilementioning

confidence: 99%

Rapeseed use in aquaculture

Adem

Tressel

Pudel

et al. 2014

OCL

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-The main problem of the aquaculture sector is the provision of suitable and sufficient fish feed, because the most important protein source in aquaculture, the fish meal, is a limited resource. Due to their high nutritional value the rapeseed proteins have great potential as an alternative protein source for the fish nutrition. Therefore, the aim of this work is to develop a manufacturing process of high quality rapeseed protein concentrates, which can replace the limited marine resource. For this purpose, small pilot scale processing procedures were performed to produce a rapeseed protein concentrate (RPC). The meal for protein extraction was prepared by gentle meal processing. Rapeseed protein fractions were prepared by an aqueous extraction procedure. The obtained protein solution is further purified and then dried. The investigated rapeseed protein extraction process provides RPC with high nutritional value and low levels of antinutritional factors. From the nutritional point of view the produced RPC can be compared with the fishmeal. Its amino acid profile reflects the amino acid demands of fish. The obtained RPC was utilized for experimental setups of fish meal replacement in diets for rainbow trout, turbot, common carp and wels catfish. Experimental results from the conducted feeding trials demonstrate an enormous potential of RPC as protein source in aquafeeds. The highest fishmeal replacement level (up to 100%) was observed in the feeding trials with rainbow trout. Therefore, especially in the nutrition of rainbow trout, RPC was identified as an excellent fishmeal alternative.

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Section: Protein Profilementioning

confidence: 99%

Rapeseed use in aquaculture

Adem

Tressel

Pudel

et al. 2014

OCL

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“…8. Far ultraviolet CD spectra of napin at room temperature and after heating to 80 "C at different pH, according to SCHWENKE et al [40] d n m l molecular mass storage proteins to which belong the 2 S proteins of Brazil nut There are some chemical and structural characteristics : the high content of sulphurcontaining amino acids, the existence of a large and a small polypeptide chain linked one to another by disulphide bonds, the high content of helical conformation. The latter has been determined for napin [8] and both for the linseed [48] and poppy seed proteins [SO] by means of circular dichroism (CD) spectroscopy.…”

Section: The Structure Of the Low-molecular Mass Basic Albumin ("Napin")mentioning

confidence: 99%

Structural studies on native and chemically modified storage proteins from rapeseed (Brassica napus L.) and related plant proteins

Schwenke

1990

Nahrung

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Recent data on the structure and chemical modification of the two main storage proteins of rapeseed, the high-molecular mass 12 S globulin and the low-molecular mass 2 S protein (napin) are summarized and compared with those of related seed proteins. The 12 S globulin is built up of six subunits forming a quaternary structure which can be approximated by the model of a trigonal antiprism. The subunits, composed of a larger and a smaller polypeptide chain each, have a two-domain structure which is typical for all related plant proteins. These are characterized by a sedimentation coefficient of 11-13 S, a molecular mass of 300,000-360,000 g/mol and a high percentage of beta-sheet conformation. Increasing succinylation results in a step-by-step dissociation up to the subunits and to an unfolding of the latter at a critical level of modification amounting to 60-70%. These structural changes affect the functional properties remarkably. The napin fraction comprises a group of closely related and highly basic proteins with molecular masses of 12,000-14,000 g/mol, a high content of sulphur-containing amino acids and rich in helical conformation. They are built up of a larger and a smaller disulphide bridged polypeptide chain. Acylation does not abolish the secondary or tertiary structure which are stabilized by inter- and intrachain disulphide bonds. Acylation results, however, in a stabilization of the protein against heat-induced aggregation.

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“…Far die Trilbungstitrations-Versuche wurde ein durch Tannin-Coffein-Behung nach [6] Der e1ektrosi:atische Charakter der Wechselwirkung zwischen Sonnenblumensamenalbumin und Alginat bzw. Pektin wird durch die gegenseitige Abhangigkeit der Hohe des Trubungsmaximums von pH-Wert und Polyanionen-Anteil (W-Wert) so-wie der Beeinflussung durch Elektrolyte ausgewiesen.…”

Section: Materials Und Methodenunclassified

Proteingewinnung unter Einsatz von komplexbildenden Stoffen. 2. Mitt. Zur Bildung unlöslicher Komplexe zwischen Sonnenblumenalbuminen und Alginat bzw. Pektin

Schwenke

Kracht

Mieth

et al. 1977

Nahrung

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The formation of insoluble complexes of sunflower seed albumin and alginate or pectin is studied by means of turbidimetric titration and by determining the pH-dependent precipitability of protein. The complex formation that is based on electrostatic interaction is a function of the pH value and the protein-polyanion ratio. Consequently, it is affected by the neutral salt content of the solutions. 90% and more of the dissolved protein may be precipitated if the proportion of the precipitant amounts to 20%. A sodium chloride content of 0.6% reduces the precipitability by alginate to 74%. In the presence of 0.3% sodium chloride, at most 55% of protein are still precipitated by pectin. The difference in strength between the albumin-alginate and the albumin-pectin complex is also expressed by the dye-binding power. Albumin-pectin complexes bind the same amount of amido black as free protein. On the contrary, albumin-alginate complexes exhibit reduced dye-binding power due to stronger binding of the protein to the polyanion. The results obtained by turbidimetric titration of model systems can, in principle, be extrapolated to the precipitation of albumins from protein extracts. In accordance with the heterogenicity of the protein, the turbidimetric titration of the albumin-alginate and the albumin-pectin complexes exhibits two maxima.

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Über Samenproteine. 3. Mitt. Isolierung und Charakterisierung der Albumine aus Sonnenblumen‐ und Rapssamen

Cited by 48 publications

References 11 publications

Rapeseed use in aquaculture

Rapeseed use in aquaculture

Structural studies on native and chemically modified storage proteins from rapeseed (Brassica napus L.) and related plant proteins

Proteingewinnung unter Einsatz von komplexbildenden Stoffen. 2. Mitt. Zur Bildung unlöslicher Komplexe zwischen Sonnenblumenalbuminen und Alginat bzw. Pektin

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