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  • Keywords: β-galactosidase; thermophilic fungus; Rhizomucor; extracellular; solid state fermentation  (1)
  • cataract Shionogi mouse  (1)
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  • 1
    ISSN: 1432-0428
    Keywords: MHC class III region ; non-obese diabetic mouse ; non-obese non-diabetic mouse ; cataract Shionogi mouse ; Type 1 (insulin-dependent) diabetes mellitus ; restriction fragment length polymorphisms
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The non-obese diabetic (NOD) mouse strain which spontaneously develops diabetes is a model for human Type 1 (insulin-dependent) diabetes mellitus. At least one of several genes controlling diabetes in the NOD mouse has been mapped to the MHC. Although previous experiments have implicated the MHC class II genes in the development of the disease, the existence of other MHC linked susceptibility genes has not been ruled out. In order to identify these susceptibility genes we have further characterized the MHC haplotype of the NOD mouse and two non-diabetic sister strains, the non-obese non-diabetic (NON) and cataract Shionogi (CTS). We have examined the mouse MHC class III region for the presence of homologous genes to 17 newly isolated human MHC class III region genes (G1, G2, G4, G6, G7a/valyl-tRNA synthetase, HSP70, G8, G9, G10, G12, G13, G14, G15, G16, G17 and G18). We detect unique hybridizing DNA fragments for 16 of the 17 genes in six inbred mouse strains (NOD, NON, CTS, B10, BALB/c and CBA/J) indicating that this part of the H-2 region is similar to the human MHC class III region. Using a panel of restriction enzymes we have defined RFLPs for 6 (G2, G6, HSP70, G12, G16, G18) of the 16 cross-hybridizing probes. The RFLPs demonstrate that NOD, NON and CTS mouse strains each have a distinct MHC haplotype in the MHC class III region.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Journal of industrial microbiology and biotechnology 19 (1997), S. 239-245 
    ISSN: 1476-5535
    Keywords: Keywords: β-galactosidase; thermophilic fungus; Rhizomucor; extracellular; solid state fermentation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: 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.
    Type of Medium: Electronic Resource
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