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  • 1
    Electronic Resource
    Electronic Resource
    Molecular inclusions. Adsorption of macromolecules on porous glass membranes (1969)
    s.l. : American Chemical Society
    Journal of the American Chemical Society 91 (1969), S. 2370-2371 
    Details
    ISSN: 1520-5126
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ja01037a030
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Immobilized glucose isomerase for the continuous conversion of glucose to fructose (1975)
    s.l. : American Chemical Society
    Journal of agricultural and food chemistry 23 (1975), S. 920-923 
    Details
    ISSN: 1520-5118
    Source: ACS Legacy Archives
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/jf60201a018
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Covalent coupling of alkaline bacillus subtilis protease to controlledpore silica with a new simplified coupling technique (1974)
    Springer
    Molecular and cellular biochemistry 4 (1974), S. 217-220 
    Details
    ISSN: 1573-4919
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary A controlled-pore silica with an average pore diameter of 510 A° was used as the carrier for the immobilization of alkaline Bacillus subtilis protease. The coupling of the enzyme was accomplished by a simple two-step procedure which involved the aqueous reaction of a bifunctional diazonium salt with the surface of the silica followed by the coupling of the enzyme through the remaining available azo functional group. The stability of the coupled enzyme was compared to that of an adsorbed enzyme produced under similar conditions. Both immobilized enzymes were stored in water at room temperature and were repeatedly assayed at intervals up to 103 days. These protease preparations were assayed with 1% casein solutions at pH 7.8 at 37°C. Under these conditions, the adsorbed enzyme exhibited a half-life of approximately 48 days, while that of the coupled protease was somewhat greater than 80 days.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01731484
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  • 4
    Electronic Resource
    Electronic Resource
    A stannous bridge for coupling urease to controlled pore titanium (1974)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 16 (1974), S. 1419-1423 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260161011
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  • 5
    Electronic Resource
    Electronic Resource
    Simultaneously immobilized glucose oxidase and catalase in controlled-pore titania (1974)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 16 (1974), S. 897-908 
    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 immobilization of glucose oxidase and catalase by adsorption within the pores of controlled-pore titania has yielded a remarkably stable enzyme system. Catalase apparently acts as both a stabilizer and an activator for glucose oxidase within the pores of this material. Hydrogen peroxide concentrations and flow rates have a marked effect upon the apparent activity of the immobilized enzyme system. The carrier parameters were varied to obtain optimum loading and stability information.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260160704
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  • 6
    Electronic Resource
    Electronic Resource
    Assay of glucose oxidase by differential conductivity (1974)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 16 (1974), S. 525-529 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260160408
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  • 7
    Electronic Resource
    Electronic Resource
    Immobilisierte Biomaterialien  -  Techniken und Anwendungen (1982)
    Weinheim : Wiley-Blackwell
    Zeitschrift für die chemische Industrie 94 (1982), S. 836-852 
    Details
    ISSN: 0044-8249
    Keywords: Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Die Immobilisierung von Enzymen, Cofaktoren und ganzen Zellen bietet die Möglichkeit, die Aktivität von Biomaterialien ökonomisch zu nutzen. Zur Immobilisierung haben sich Adsorption und kovalente Bindung an hochmolekulare Träger sowie Einschluß in Polymere und Mikroverkapselung bewährt. Will man Systeme mit immobilisierten Biomaterialien entwickeln, muß man sowohl biochemische und kinetische als auch apparative Aspekte berücksichtigen. Beispiele für großtechnische Anwendungen sind die Gewinnung von Fructose-reichem Sirup aus Stärke und die Herstellung von L-Aminosäuren durch selektive Hydrolyse von N-Acyl-DL-aminosäuren.
    Additional Material: 19 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/ange.19820941104
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  • 8
    Electronic Resource
    Electronic Resource
    Immobilized Biomaterials - Techniques and Applications (1982)
    Weinheim : Wiley-Blackwell
    Angewandte Chemie International Edition in English 21 (1982), S. 837-854 
    Details
    ISSN: 0570-0833
    Keywords: Enzymes ; Cofactors ; Biotechnology ; Immobilization ; Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The immobilization of enzymes, cofactors and whole cells offers the potential of economical exploitation of biomaterial activity. Enzymes or cells can be immobilized by binding to carriers through adsorption or covalent linkages or by entrapment in a polymer matrix or microencapsulation. The development of immobilized biomaterial systems requires the involvement of biochemical, kinetics and reactor design principles. Examples of commercial scale applications of immobilized biomaterial systems are the production of a fructose-rich syrup from starch and the synthesis of L-amino acids by selective hydrolysis of N-acyl-D,L-amino acids.
    Additional Material: 19 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/anie.198208371
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