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Starches Aspergillus niger

Only Aspergillus niger is strongly amylolytic and capable of using foe starch in the effluent. Open lagoon systems operating at low pH, if effective, would be a cheaper method of production than aseptic bioreactors. [Pg.350]

The efficiency in raw cassava starch hydrolyzation of pectinases from Rhizopus sp. 26R compared with a commercial pectinase when mixed with Glucoamylase from Aspergillus niger J8. [Pg.858]

Figure 9 Pectinases from Rhizopus sp. 26R showed high potential in enhancing the digestion of raw starch from ground cassava tuber when the enzymes were mixed with the glucoamylase of Aspergillus niger J8... Figure 9 Pectinases from Rhizopus sp. 26R showed high potential in enhancing the digestion of raw starch from ground cassava tuber when the enzymes were mixed with the glucoamylase of Aspergillus niger J8...
Morris, V. J., Gunning, A. P., Faulds, C. B., Williamson, G., and Svensson, B. (2005). AFM images of complexes between amylose and Aspergillus niger glucoamylase mutants, native, and mutant starch binding domains A model for the action of glucoamylase. Starch-Starke 57,1-7. [Pg.239]

Abraham TE, Jamuna R, Bansilal CV, Ramakrishna SV (1991) Continuous synthesis of glucoamylase by immobilized fungal mycelium of Aspergillus niger. Starch-Starke 43 113-116... [Pg.179]

Haq, L, Ali, S., Iqbal, J. (2003). Direct production of citric acid from raw starch by Aspergillus niger. Process Biochem., 38, 921-924. [Pg.459]

Figure 7.10 Schematic representation of the domain structure of glucoamylases Aspergillus niger glucoamylase-1, with starch-binding, linker and catalytic domains Aspergillus mger glucoarriylase-2, with only the catalytic domain Rhizopus nievus glucoamylase-l, with starch binding, linker and catalytic domains... Figure 7.10 Schematic representation of the domain structure of glucoamylases Aspergillus niger glucoamylase-1, with starch-binding, linker and catalytic domains Aspergillus mger glucoarriylase-2, with only the catalytic domain Rhizopus nievus glucoamylase-l, with starch binding, linker and catalytic domains...
Application and Principle This procedure is used to determine the a-amylase activity of enzyme preparations derived from Aspergillus niger var. Aspergillus oryzae var. Rhizopus oryzae var. and barley malt. The assay is based on the time required to obtain a standard degree of hydrolysis of a starch solution at 30° 0.1°. The degree of hydrolysis is determined by comparing the iodine color of the hydrolysate with that of a standard. [Pg.900]

Growth of Aspergillus niger NRRL 326 on starch gives a product (insoluble in hot water), termed pseudonigeran, which contains predominant a-D-(l— 3)-linkages (87%) and some a-D-(l— 4)-linkages... [Pg.375]

Aspergillus niger spore germination time as a function of a and NMR in small carbohy-drates starch (1 9 ratio) systems at various a . Relative intensity expressed as NMR active (detected) water. [Pg.180]


See other pages where Starches Aspergillus niger is mentioned: [Pg.715]    [Pg.716]    [Pg.853]    [Pg.854]    [Pg.858]    [Pg.231]    [Pg.239]    [Pg.59]    [Pg.84]    [Pg.460]    [Pg.300]    [Pg.515]    [Pg.290]    [Pg.1538]    [Pg.244]    [Pg.489]    [Pg.612]    [Pg.548]    [Pg.368]    [Pg.17]    [Pg.1379]    [Pg.1379]    [Pg.148]    [Pg.19]    [Pg.368]    [Pg.374]    [Pg.1452]    [Pg.2357]    [Pg.98]    [Pg.1373]    [Pg.177]    [Pg.179]    [Pg.548]    [Pg.417]    [Pg.254]   
See also in sourсe #XX -- [ Pg.170 , Pg.177 , Pg.178 , Pg.179 , Pg.180 ]




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Aspergillus niger starch hydrolysis

Niger

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