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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    European food research and technology 210 (1999), S. 119-122 
    ISSN: 1438-2385
    Keywords: Key words Rheology ; Wheat flour ; Rapid Visco Analyser
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract  The blended dough made from raw wheat flour and wheat flour steamed for 15 min at a ratio of 1 : 1, along with minor ingredients (salt, oil) showed reduced farinograph water absorption capacity. The stability of the blended dough with oil was reduced while the mixing tolerance index increased. The inclusion of salt in the blend increased the resistance to extension and also the area under the curve. The hardness and cohesiveness measured by means of texture profile analysis decreased with the inclusion of oil in the blend, while increasing with the addition of salt. The Rapid Visco Analyser used to measure pasting characteristics showed a peak viscosity which increased for the blend with salt, but decreased for that with oil. Similarly, the hot paste viscosity, cold paste viscosity and area under the curve increased for the blend with salt, but decreased for the blend with oil.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-2048
    Keywords: Cell wall ; Extensin ; Extensin peroxidase ; Hydroxyproline-rich glycoprotein ; Lycopersicon (cell culture)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Extensin, a hydroxyproline-rich glycoprotein comprising substantial amounts of β-l-arabinose-hydroxyproline glycosidic linkages is believed to be insolubilized in the cell wall during host-pathogen interaction by a peroxidase/hydroperoxide-mediated cross-linking process. Both extensin precursor and extensin peroxidase were ionically eluted from intact water-washed tomato (hybrid) of Lycopersicon esculentum Mill. and L. peruvianum L. (Mill.) cells in suspension cultures and purified to homogeneity by a rapid and simple procedure under mild and non-destructive experimental conditions. The molecular weight of native extensin precursor was estimated to be greater than 240–300 kDa by Superose-12 gel-filtration chromatography. Extensin monomers have previously been designated a molecular weight of approximately 80 kDa. Our results indicate that salt-eluted extensin precursor is not monomeric. Agarose-gel electrophoresis, Superose-12-gel-filtration, extensin-peroxidase-catalysed cross-linking, Mono-S ion-exchange fast protein liquid chromatography (FPLC), and peptide-sequencing data confirmed the homogeneity of the extensin preparation. Evidence that the purified protein was extensin is attributed to the presence of the putative sequence motif — Ser (Hyp)4 — within the N-terminal end of the protein. Treatment of extensin with trifluoroacetic acid demonstrated that arabinose was the principal carbohydrate. The amino-acid composition of the purified extensin was similar to those reported in the literature. The cross-linking of extensin in vitro upon incubation with extensin peroxidase and exogenous H2O2 was characteristic of other reported extensins. Furthermore, Mono-S ion-exchange FPLC of native extensin precursor resolved it into two isoforms, A (90%) and B (10%). The amino-acid compositions of extensin A and extensin B were found to be similar to each other and both extensins were cross-linked in vitro by extensin peroxidase.
    Type of Medium: Electronic Resource
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