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  • 1
    Electronic Resource
    Electronic Resource
    Effects of norfloxacin on the retina in rabbits (1995)
    Springer
    Graefe's archive for clinical and experimental ophthalmology 233 (1995), S. 173-180 
    Details
    ISSN: 1435-702X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract • Background: Fluoroquinolones have a strong affinity with melanin, and their ocular effects have been reevaluated. Norfloxacin, one of the fluoroquinolones, has broad-spectrum activity against aerobic gram-positive and gram-negative bacteria. We examined the retinal toxicity and intraocular pharmacokinetics of intravitreal norfloxacin in rabbits. • Methods: Twenty-three albino and 23 pigmented rabbits were divided into three groups to evaluate retinal toxicity and two groups to investigate the intraocular pharmacokinetics. Each of these five groups was further divided into two subgroups (albino rabbits and pigmented rabbits). • Results: With 500 Etg norfloxacin, the oscillatory potential of the electroretinogram was transiently and selectively deteriorated in albino and pigmented rabbits, whereas the electroretinogram remained unchanged with 50 μg in pigmented rabbits. No changes were observed in the visual evoked potential or on histology of the retina 7 days after an intravitreal injection of 50 or 500 ltg norfloxacin. The electroretinogram and the retinal histology became abnormal 7 days after four intravitreal injections of 500 μg norfloxacin at 7-day intervals. As regards the intraocular pharmacokinetics after an intravitreal injection, the norfloxacin concentration in the chorioretina was as high as that in the vitreous 3 h after injection and was much higher than that in the vitreous 7 days after injection. Similar results were obtained after multiple injections. • Conclusion: These results indicate a high concentration of norfloxacin in the melanin-containing ocular tissues.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00166611
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  • 2
    Electronic Resource
    Electronic Resource
    Ethanol fermentation of raw cassava starch with Rhizopus koji in a gas circulation type fermentor (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 27 (1985), S. 1270-1273 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Studies have been conducted in a gas circulation type fermentor in order to characterize the ethanol fermentation of uncooked cassava starch with Rhizopus koji. Results showed that ethanol concentration reached 13-14% (v/v) in 4-day broth, and the maximum productivity of ethanol was 2.3 g ethanol/L broth h. This productivity was about 50% compared to the productivity of a glucose-yeast system. Ethanol yield reached 83.5-72.3% of the theoretical yield for the cassava starch used. The fermentor used in the present work has been proven by experiment to be suitable for ethanol fermentation of the broth with solid substrate.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260270823
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Continuous production of maltotetraose using a dual immobilized enzyme system of maltotetraose-forming amylase and pullulanase (1990)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 36 (1990), S. 790-796 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: In order to produce a product with a high content of maltotetraose, dual-enzyme systems composed of immobilized maltotetraose-forming amylase (G4-forming amylase) and pullulanase were studied. The thermostability of individually immobilized enzymes was examined in continuous operation; studies revealed that the enzyme immobilized on “Chitopearl” was much more stable than that immobilized on Diaion HP-50. The effects of operating conditions on the stability of G4 forming amylase immobilized on “Chitopearl” were examined to confirm that the apparent half-life data could be arranged using the immobilized enzyme stability factor, fs. As for the dual immobilized enzyme system, six methods of usage were considered, with five yielding a 7-10% (w/w) higher content of maltotetraose product than the single-enzyme system. The effects of operating conditions on the maltotetraose production reaction were examined to confirm that the maltotetraose content of the products could be analyzed using the specific space velocity,SSV. In dual immobilized enzyme systems, pullulanase immobilized on the same carrier as the G4-forming amylase was found to be more stable than pullulanase immobilized on separate carriers. The effectiveness of using immobilized pullulanase along with the G4-forming amylase was confirmed from constant-conversion operations in which the maltotetraose content in the product was kept at 50% (w/w) in laboratory-scale experimentation.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260360806
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  • 4
    Electronic Resource
    Electronic Resource
    Continuous production of maltotetraose using immobilized Pseudomonas stutzeri amylase (1988)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 32 (1988), S. 669-676 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A continuous production process of maltotetraose was investigated by using immobilized maltotetraose (G4)- forming amylase (1,4-α-D-glucan maltotetraohydrolase, EC3.2.1.60) from Pseudomonas stutzeri adsorbed on a macroporous hydrophobic resin. The maximum reaction rate was obtained at 55°C and the activation energy of hydrolysis by immobilized G4-forming amylase was calculated to be 8.45 kcal/mol. The maltotetraose yield was greatly influenced by the flow rate of substrate solution, its concentration, and the immobilized enzyme activity. The newly defined factor “specific space velocity” was successfully introduced to normalize the operating parameters. Using this factor, the immobilized enzyme reactor then can be simulated and the operating dynamics can be determined.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260320512
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  • 5
    Electronic Resource
    Electronic Resource
    Stability of immobilized maltotetraose-forming amylase from Pseudomonas stutzeri (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 33 (1989), S. 845-855 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The stability of immobilized maltotetraose (G4)-forming amylase (1,4-α-D-glucan maltoteraohydrolase, EC 3.2.1.60) from Pseudomonas stutzeri was investigated in both batch and continous processes. The inactivation process of the immobilized enzyme seemed to obey first-order kinetics, and the immobilized enzyme became more stable when coexisting with 20-30 wt % substrate and calcium ions. From intensive studies on the operational stability in the continuous process, the apparent half-life of G4 productivity in a constant-flow system was mainly affected by the reaction temperature, substrate concentration, and initial immobilized enzyme activity. A new factor, immobilized enzyme stability factor fs, was proposed to evaluate the half-life of the immobilized enzyme system.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260330708
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