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Comparison of ethanol-soluble proteins from different rye (Secale cereale) varieties by two-dimensional electrophoresis.

The major storage proteins from six rye varieties, grown under the same conditions in 1997 and 1998 in Rønhave, Denmark, were analyzed by two-dimensional (2-D) polyacrylamide gel electrophoresis. The proteins were extracted from ground rye kernels with 70% ethanol and separated by 2-D electrophoresis. The gels were scanned, compared using ImageMaster software and the data sets were analyzed by principal component analysis (PCA) using THE UNSCRAMBLER software. Afterwards MATLAB was used to make a cluster analysis of the varieties based on PCA. The analysis of the gels showed, that the protein patterns (number of different proteins and their isoelectric points and molecular weights) from the six rye varieties were different. Based on the presence of unique cultivar-specific spots it was possible to differentiate between all six varieties if the two harvest years were investigated separately. When the results were combined from the two years five varieties could be differentiated. The results from the PCA confirmed the finding of the unique spots and cluster analysis was made in order to illustrate the results. The combination of the results from 2-D electrophoresis and other grain characteristics showed that one protein spot was located close to the parameters bread volume and bread height.

Electrophoresis, Gel, Two-Dimensional↗

Mycotoxins in cereal grain. Part III. Production of ochratoxin A in different varieties of wheat, rye and barley.

Kernels of several varieties of wheat, rye and barley were found to have different resistance to fungi attack and ochratoxin A production, particularly in first step of fungus development on kernels. Zinc was stated to be a limiting factor of ochratoxin production. viable sound kernels were very resistant against fungi. Dead (e.g. autoclaved) kernels were attacked by fungus very quickly. Varieties with stronger resistance to fungi invasion during storage were selected.

Aspergillus↗

Mycotoxins in cereal grain. Part VI. The effect of ochratoxin A on growth and tissue residues of the mycotoxin in broiler chickens.

Eight weeks experiment on effects of continuous feeding of mycotoxin graded levels (0; 9.5; 1.0; .5; 2.0 mg ochratoxin A (OA) per kilogram of feed) to male and female broiler chickens was carried out. Birds' mortality was similar in all groups including control. Macroscopical veterinary examination did not reveal any changes in livers and kidneys. Males were found to be more sensitive to OA than females. The depression of body weight was found to be proportional to level of OA. The reduction of body weight of males (30%) was more significant than that of females (20%). Feed consumption per one kilogram of body weight was dependent on OA concentration in feed. In livers and white muscles of birds fed 1.0; 1.5 and 2.0 mg OA/kg feed and in red muscles of birds fed 1.5 and 2.0 mg OA/kg feed residues of OA were observed. OA disappeared completely from all mentioned tissues after 4 days when birds were fed with OA free feed.

Animal Feed↗

Thermal degradation of precursors and formation of flavour compounds during heating of cereal products. Part II. The formation and changes of volatile flavour compounds in thermally treated malt extracts at different temperature and pH1.

The effect of temperature and pH on the formation and changes of volatile flavour compounds in thermally treated malt extracts was studied. The dependence of thermal treatment parameters on organoleptic properties of the extracts was stated. Alkaline pH of the medium was found to promote the formation of the compounds yielding a caramel odour. The most desirable organoleptic characteristics were obtained at pH 4.0-5.5 and temperature 140 degrees C. Thirty compounds typical for nonenzymatic browning were identified.

Chromatography, Gas↗

Mycotoxins in cereal grain. Part 13. Deoxynivalenol and 3-acetyl-deoxynivalenol in wheat kernels and chaff with head fusariosis symptoms.

In the period of harvest at 1987 field samples of wheat heads with fusariosis symptoms were collected in 18 provinces of Poland. Subsamples of heads infected with Fusarium culmorum (W.G.Sm) Sacc. and Fusarium graminearum Schwabe were analyzed for Fusarium metabolites. In fractions of kernels with visible Fusarium-damage deoxynivalenol (DON) was present in average amount of 18.7 mg/kg (range 9.6-25.3 mg/kg) and 3-acetyl DON 1.9 mg/kg. Fractions of kernels without symptoms of visible Fusarium-damage contained only DON at average 2 mg/kg (range 0.8-3.6 mg/kg). A method of approximate calculation of DON content in a given lot of grain is proposed which may be realized during samples grading.

Food Contamination↗

Mycotoxins in cereal grain. Part 14. Histochemical examination of Fusarium-damaged wheat kernels.

Wheat kernels with visible Fusarium-damage, naturally infected, have been examined with histochemical techniques to observe mycelium growth inside kernels and change in kernels cells. Kernels infected with F. culmorum were found to be damaged more extensively, comparatively to those infected with F. graminearum, F. avenaceum and F. nivale/(Microdochium nivale). Growth of Fusarium mycelium was most abundant between pericarp and aleurone layer and alongside of scutellum. Mycelium colonized also endosperm and embryo--both plumula and radicula.

Fusarium↗

[The determination of protein hydrophobicity. 1. Determination of the hydrophobicity of selected cereal and milk proteins using their sodium dodecyl sulfate binding capacities].

The sodium dodecylsulphate (SDS) binding capacities of secalin, gliadin and gluten in the presence of a very low SDS concentration were determined and compared to the SDS binding capacities of bovine serum albumin (BSA), beta-lactoglobulin, ovalbumin und beta-casein. The SDS binding capacities of endosperm proteins determined in phosphate buffer (pH 6.0) are very low. Only 0.6 microgram .. 0.8 microgram SDS were bound to 500 micrograms of the proteins. This low SDS binding capacities do not correlate with the expected hydrophobicity of these proteins. In comparison, 500 micrograms of ovalbumin, beta-lactoglobulin and BSA each bind 0.5, 5.9 and 13.5 micrograms SDS, respectively. According to literature the SDS binding capacities of these proteins are in correlation with the surface hydrophobicity determined with cis-parinaric acid using the fluorescence probe method. The SDS binding capacities of endosperm proteins increased in the presence of 0.1 N acetic acid and consequently 6.2 micrograms .. 6.9 micrograms SDS were bound to 500 micrograms of the corresponding proteins. beta-casein described as a highly hydrophobic protein binds only 0.9 micrograms SDS to 500 micrograms of it in phosphate puffer (pH 6.0) and 1.2 micrograms SDS in 0.1 N acetic acid, respectively.

Chemical Phenomena↗

Short tandem repeats shared by B- and C-hordein cDNAs suggest a common evolutionary origin for two groups of cereal storage protein genes.

We have identified cDNA clones coding for the major sulphur-rich and sulphur-poor groups of barley storage proteins (the B- and C-hordeins, respectively). Hybridization studies have revealed unexpected homologies between B- and C-hordein mRNAs. Using a deletion mutant (Risø 56), we have mapped some C-hordein-related sequences within, or closely associated with, B-hordein genes at the Hor 2 locus. Nucleotide sequencing has shown that the primary structure of B-hordein polypeptides can be divided into at least two domains: domain 1 (repetitive, proline-rich, sulphur-poor), which is homologous to C-hordein sequences, and domain 2 (non-repetitive, proline-poor, sulphur rich), which makes up two-thirds of the polypeptide and is partially homologous to a 2S globulin storage protein found in dicotyledons. The coding sequences that are homologous in B- and C-hordein mRNAs have an asymmetric base composition (>80% C-A) and are largely composed of a degenerate tandem repeat based on a 24 nucleotide consensus that encodes Pro-Gln-Gln-Pro-Phe-Pro-Gln-Gln. We discuss the evolutionary implications of the domain structure of the B-hordeins and the unusual relationship between the two groups of barley storage proteins.

Amino Acid Sequence↗