Wheat Germ (wheat + germ)

Distribution by Scientific Domains

Terms modified by Wheat Germ

  • wheat germ agglutinin

  • Selected Abstracts


    Use of a spouted bed to improve the storage stability of wheat germ followed in paper and polyethlyene packages

    JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE, Issue 8 2005
    Füsun Yöndem-Makasc
    Abstract Stabilization of wheat germ by heating in a spouted bed for 180,540 s with air at 140,200 °C was studied. The lipase activity decreased by 6,65%. Wheat germ processed at 200 °C for 360 s was ranked highest in sensory evaluation, described as having ,a golden color' and ,nutty flavor', and its lipoxygenase activity had decreased by 91.2%. This product and raw wheat germ were stored in paper, polyethylene and vacuum-packed polyethylene pouches at 5 °C, room temperature (18,26 °C) and 40 °C, and the moisture contents, water activities, free fatty acid contents and peroxide values were followed for 20 weeks. The increases were faster in paper pouches than in the polyethylene ones; vacuum packaging in polyethylene did not bring about significant improvement. The peroxide values of raw samples exceeded 10 meq O2 kg,1 oil after 3,23 days while those of the processed samples stored at room temperature or 5 °C were still less than 10 after 20 weeks. The free fatty acid content and peroxide value changes were expressed by zero order kinetics, resulting in similar activation energies for the raw and processed samples. Copyright © 2005 Society of Chemical Industry [source]


    Characterization of hydroxyaromatic compounds in vegetable oils by capillary electrophoresis with direct injection in an oil-miscible KOH/propanol/methanol medium

    ELECTROPHORESIS, Issue 17 2005
    Carla R. B. Mendonça
    Abstract The separation of hydroxyaromatic compounds in vegetable oils, including synthetic antioxidants (3- tert -butyl-4-hydroxyanisol and 2,6-di- tert -butyl-4-hydroxytoluene), E-vitamers and other natural oil components, by nonaqueous capillary electrophoresis in an oil-miscible background electrolyte (BGE) was investigated. The BGE contained 40,mM KOH in a methanol/1-propanol (PrOH) mixture (15:85 v/v). The oil samples were 1:1 diluted with PrOH and directly injected in the capillary. Under negative polarity (cathode at the injection end), the anionic solutes moved faster than the electroosmotic flow, being well-resolved among them and from the triacylglycerols. Using virgin palm, extra virgin olive, wheat germ, virgin soybean and other oils, the capability of the procedure to quickly yield a characteristic profile of the biophenols present in the sample was demonstrated. The , -, (,,+,,)- (as unresolved pair) and , -tocopherols of a soybean oil sample were quantified. [source]


    Transcriptional signatures in response to wheat germ agglutinin and starvation in Drosophila melanogaster larval midgut

    INSECT MOLECULAR BIOLOGY, Issue 1 2009
    H.-M. Li
    Abstract One function of plant lectins such as wheat germ agglutinin is to serve as defences against herbivorous insects. The midgut is one critical site affected by dietary lectins. We observed marked cellular, structural and gene expression changes in the midguts of Drosophila melanogaster third instar larvae that were fed wheat germ agglutinin. Some of these changes were similar to those observed in the midguts of starved D. melanogaster. Dietary wheat germ agglutinin caused shortening, branching, swelling, distortion and in some cases disintegration of the midgut microvilli. Starvation was accompanied primarily by shortening of the microvilli. Microarray analyses revealed that dietary wheat germ agglutinin evoked differential expression of 61 transcripts; seven of these were also differentially expressed in starved D. melanogaster. The differentially transcribed gene clusters in wheat germ agglutinin-fed larvae were associated with (1) cytoskeleton organization; (2) digestive enzymes; (3) detoxification reactions; and (4) energy metabolism. Four possible transcription factor binding motifs were associated with the differentially expressed genes. One of these exhibited substantial similarity to MyoD, a transcription factor binding motif associated with cellular structures in mammals. These results are consistent with the hypothesis that wheat germ agglutinin caused a starvation-like effect and structural changes of midgut cells of D. melanogaster third-instar larvae. [source]


    Identification of antigenic targets of paraproteins by expression cloning does not support a causal role of chronic antigenic stimulation in the pathogenesis of multiple myeloma and MGUS

    INTERNATIONAL JOURNAL OF CANCER, Issue 2 2007
    Klaus-Dieter Preuss
    Abstract Antigenic targets of monoclonal gammopathy of undetermined significance (MGUS) and multiple myeloma (MM) paraproteins have been suggested to play an important role as growth stimulators in the pathogenesis of these neoplasms. To identify such targets, we screened cDNA libraries from human testis, lung and breast cancer, bovine and porcine muscle and wheat germ for reactivity with paraproteins in the sera from 115 patients with MGUS and MM. Of >6 × 108 paraprotein,antigen interactions screened, an IgA paraprotein from a female patient bound to sperm-specific cylicin-2, and 3 IgG paraproteins bound to tripeptidyl-peptidase-II (TPP-2), insulin-like growth-factor binding-protein-2 (IGFBP-2) and porcine kinesin. Specificity was confirmed by reverse Western blots using recombinant antigens. The broad spectrum of auto-, allo- and heteroantigens as targets of human paraproteins in patients without signs of chronic antigenic stimulation renders a causal role of the antigenic stimulus in the pathogenesis of MGUS and MM unlikely. © 2007 Wiley-Liss, Inc. [source]


    Use of a spouted bed to improve the storage stability of wheat germ followed in paper and polyethlyene packages

    JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE, Issue 8 2005
    Füsun Yöndem-Makasc
    Abstract Stabilization of wheat germ by heating in a spouted bed for 180,540 s with air at 140,200 °C was studied. The lipase activity decreased by 6,65%. Wheat germ processed at 200 °C for 360 s was ranked highest in sensory evaluation, described as having ,a golden color' and ,nutty flavor', and its lipoxygenase activity had decreased by 91.2%. This product and raw wheat germ were stored in paper, polyethylene and vacuum-packed polyethylene pouches at 5 °C, room temperature (18,26 °C) and 40 °C, and the moisture contents, water activities, free fatty acid contents and peroxide values were followed for 20 weeks. The increases were faster in paper pouches than in the polyethylene ones; vacuum packaging in polyethylene did not bring about significant improvement. The peroxide values of raw samples exceeded 10 meq O2 kg,1 oil after 3,23 days while those of the processed samples stored at room temperature or 5 °C were still less than 10 after 20 weeks. The free fatty acid content and peroxide value changes were expressed by zero order kinetics, resulting in similar activation energies for the raw and processed samples. Copyright © 2005 Society of Chemical Industry [source]


    Crystallization and preliminary X-ray diffraction analysis of protein l -isoaspartyl O -­methyltransferase from wheat germ

    ACTA CRYSTALLOGRAPHICA SECTION D, Issue 2 2001
    Michelle D. Amaral
    Wheat-germ protein l -isoaspartyl O -methyltransferase (WPIMT) can initiate the conversion of l -isoaspartyl residues in a protein or peptide, which accumulate during the aging process in wheat-germ seeds, to normal l -aspartyl groups. The recombinant protein of WPIMT was overexpressed in Escherichia coli and purified to homogeneity. The protein was crystallized in the presence of S -­adenosine- l -homocysteine using 2-methyl-2,4-pentanediol. Preliminary X-ray analysis indicated a tetragonal space group P41212 or P43212, with unit-cell parameters a = b = 77.3, c = 152.9,Å for cryofrozen crystals at 90,K. The crystals diffracted to 3.3,Å and contain two molecules per asymmetric unit. [source]


    Treatment of Germinated Wheat to Increase Levels of GABA and IP6 Catalyzed by Endogenous Enzymes

    BIOTECHNOLOGY PROGRESS, Issue 2 2005
    Hiroyuki Nagaoka
    We found that the levels of bioactive products from wheat can be increased dramatically by manipulating germination conditions and taking advantage of the activity of endogenous enzymes. The yield of phytic acid (IP6) from wheat germinated in the presence of high, controlled levels of dissolved oxygen (188 ± 28 mg/100 g wheat) was almost three times greater than that from wheat germinated with no supplemental oxygen (74 ± 10 mg/100 g wheat). The yield of ,-aminobutyric acid (GABA) from wheat germinated in the presence of uncontrolled levels of dissolved oxygen was 18 ± 3 times greater than that from nonsupplemented wheat (1 mg/100 g wheat). The concentration of GABA was much greater in wheat germ than in whole wheat, and the yield of GABA from wheat germ processed with supplemental water (163 ± 7 mg/100 g wheat germ) was notably greater than that from wheat germ processed with no supplemental water (100 ± 2 mg/100 g wheat germ). In contrast, IP6 was more concentrated in wheat bran, and the yield of IP6 from wheat bran processed with supplemental water (3100 ± 12 mg/100 g wheat bran) was notably higher than that from wheat bran processed with no supplemental water (2420 ± 13 mg/100 g wheat bran). We conclude that the large amount of GABA extracted from wheat germ is likely due to high glutamate decarboxylase activity and low aminotransferase activity and that the large amount of IP6 extracted from wheat bran is likely due to high levels of tyrosinase activity. Our findings indicate that bioactive molecules such as GABA and IP6 can be successfully mass-produced by taking advantage of endogenous enzymatic activities. [source]


    Macroaffinity Ligand-Facilitated Three-Phase Partitioning (MLFTPP) of ,-Amylases Using a Modified Alginate

    BIOTECHNOLOGY PROGRESS, Issue 2 2003
    Kalyani Mondal
    The crude extracts of ,-amylases when mixed with alginate, tert -butyl alcohol, and ammonium sulfate resulted in an interfacial precipitate containing polymer-bound amylase. The precipitate was dissolved in 1 M maltose to recover ,-amylase activity. The recovery of ,-amylases were 74%, 77%, and 92% in the case of Bacillus amyloliquefaciens, wheat germ, and porcine pancreas, respectively. All purified preparations showed a single band on SDS-PAGE. [source]