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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    European food research and technology 210 (2000), S. 293-298 
    ISSN: 1438-2385
    Keywords: Key words Rheology ; Gel mobility ; Rapid visco analyser
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract  Blending of native wheat flour (NWF) and steamed wheat flour (SWF) in the ratio of 1 : 1was found to give good binding between the filling and coating, and improve the overall quality of the coated products. The apparent viscosity increased with increase in batter concentration (30, 33 and 36%) of all the three blends, namely NWF+SWF (5 min steaming period), NWF+SWF (15 min steaming period) and NWF+SWF(30 min steaming period). The yield stress and consistency index also increased with increase in batter concentration for all three blends. The gel mobility increased with increased steaming period of the blends. The rapid visco analyser used for measuring the pasting characteristics of the blends showed an increase in peak viscosity from 218 to 243 rapid visco units (RVU), in hot pasteviscosity from 81 to 100 RVU and in cold paste viscosity from 175 to 185 RVU. The area under the curve also increased from 1963 to 2134 RVU/min for the blends when compared with native wheat flour.
    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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