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  • Keywords: β-galactosidase; thermophilic fungus; Rhizomucor; extracellular; solid state fermentation  (1)
  • Metallonitroporphines  (1)
  • grafting  (1)
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  • 1
    Digitale Medien
    Digitale Medien
    Springer
    Catalysis letters 24 (1994), S. 79-83 
    ISSN: 1572-879X
    Schlagwort(e): Metallonitroporphines ; oxidation ; isobutane ; propane
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Chemie und Pharmazie
    Notizen: Abstract Introducing nitro groups into themeso-positions of a metalloporphyrin converts a catalytically inactive complex into a highly active catalyst for the oxidation of alkanes with molecular oxygen. The degree of nitration correlates with both the Fe(III)/Fe(II) reduction potential and the catalytic activity.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Springer
    Journal of industrial microbiology and biotechnology 19 (1997), S. 239-245 
    ISSN: 1476-5535
    Schlagwort(e): Keywords: β-galactosidase; thermophilic fungus; Rhizomucor; extracellular; solid state fermentation
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Werkstoffwissenschaften, Fertigungsverfahren, Fertigung
    Notizen: A thermostable β-galactosidase was produced extracellularly by a thermophilic Rhizomucor sp, with maximum enzyme activity (0.21 U mg−1) after 4 days under submerged fermentation condition (SmF). Solid state fermentation (SSF) resulted in a nine-fold increase in enzyme activity (2.04 U mg−1). The temperature range for production of the enzyme was 38–55°C with maximum activity at 45°C. The optimum pH and temperature for the partially purified enzyme was 4.5 and 60°C, respectively. The enzyme retained its original activity on incubation at 60°C up to 1 h. Divalent cations like Co2+, Mn2+, Fe2+ and Zn2+ had strong inhibitory effects on the enzyme activity. The K m and V max for p-nitrophenyl-β- D-galactopyranoside and o-nitrophenyl-β - D-galactopyranoside were 0.39 mM, 0.785 mM and 232.1 mmol min−1 mg−1 respectively. The K m and V max for the natural substrate lactose were 66.66 μM and 0.20 μ mol min−1 mg−1.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 3
    ISSN: 1573-8272
    Schlagwort(e): XAD-16 and NPA-1 ; invertase ; α-glucosidase ; grafting ; ultrasonic irradiation ; adsorption ; desorption ; enrichment factors
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Werkstoffwissenschaften, Fertigungsverfahren, Fertigung
    Notizen: Abstract In the present work Amberlite® XAD-16 and Indion® NPA-1, Polystyrene Divinylbenzene macroreticular spherical resins, have been evaluated quantitatively as supports for the adsorption and isolation of the yeast proteins and the enzymes, invertase and α-glucosidase. Modification of these supports has been carried out by surface grafting using acrylate polymers to reduce the hydrophobicity and nonspecific adsorption of proteins. Good grafting efficiency, in excess of 90%, has been obtained using ultrasonic irradiation for the surface activation of polystyrene resins. XAD-16 has higher adsorption capacities for the total yeast proteins as well as for both the enzymes, α-glucosidase and invertase, than NPA-1 in its respective native and grafted form. Adsorption capacities of XAD-16 and NPA-1 in their respectivenative and grafted forms for α-glucosidase are higher than the capacities for invertase. Nonspecific adsorption of total proteins has been reduced considerably after the grafting of acrylate polymers on hydrophobic supports. At the same time selectivity for the adsorption of both the enzymes has been enhanced on grafted supports. The overall solid-liquid adsorption mass transfer coefficient values (K l a) estimated for adsorption of invertase on XAD are lower than those for α-glucosidase. Native and grafted resins could be regenerated and reused for adsorption of α-glucosidase for two regeneration cycles studied. Storage stability of invertase and α-glucosidase is the same on native and grafted form of XAD-16 and is more than the enzymes in the free form.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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