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  • Biochemistry and Biotechnology
  • 1980-1984
  • 1975-1979  (199)
  • 1979  (199)
  • 1
    Electronic Resource
    Electronic Resource
    Masthead (1979)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 21 (1979) 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260210101
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  • 2
    Electronic Resource
    Electronic Resource
    Immobilized glucose oxidase-catalase and their deactivation in a differential-bed loop reactor (1979)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 21 (1979), S. 89-109 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Glucose oxidase containing catalase was immobilized with a copolymer of phenylenediamine and glutaraldehyde on pumice and titania carrier to study the enzymatic oxidation of glucose in a differential-bed loop reactor. The reaction rate was found to be first order with respect to the concentration of limiting oxygen substrate, suggesting a strong external mass-transfer resistance for all the flow rates used. The partial pressure of oxygen was varied from 21.3 up to 202.6 kPa. The use of a differential-bed loop reactor for the determination of the active enzyme concentration in the catalyst with negligible internal pore diffusion resistance is shown. Catalyst deactivation was studied, especially with respect to the presence of catalase. It is believed that the hydrogen peroxide formed in the oxidation reaction deactivates catalase first; if an excess of catalase is present, the deactivation of glucose oxidase remains small. The mathematical model subsequently developed adequately describes the experimental results.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260210108
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  • 3
    Electronic Resource
    Electronic Resource
    Masthead (1979)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 21 (1979) 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260210201
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  • 4
    Electronic Resource
    Electronic Resource
    Affinity chromatography of endoglucanase of Trichoderma viride by concanavalin A-agarose (1979)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 21 (1979), S. 167-171 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Endoglucanase (Cx cellulase) and cellobiase are often cross-contaminated in separation procedures by ion-exchange chromatography such as DEAE-cellulose. By using concanavalin A (Con A)-agarose chromatography, Cx cellulase and cellobiase from Trichoderma viride can be separated. Cx cellulase showed affinity toward Con A, indicating a glycoprotein containing α-D-mannopyransyl and α-D-glucopyranosyl end groups or internal 2-O-D-mannopyranosyl residues in sugar moieties. This method provides a way to estimate the quantities of Cx enzyme produced by T. viride and possibly by other organisms.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260210203
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  • 5
    Electronic Resource
    Electronic Resource
    Biological particles of given size, shape, and density for use in biological reactorsSee Refs. 1-4. (1979)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 21 (1979), S. 193-200 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Novel biomass support particles containing growing cells have been developed for use in large-scale fermentation processes. The characteristic size of the entrapped biomass is identical to that of the physical structure of the support particle, and particles can be produced of any size, shape, and density with a wide variety of microorganisms. Use of the particles in fermentors leads to high biomass concentration independent of throughput, predetermined biomass concentrations, the use of novel types of fermentor with advantageous performance characteristics, possibilities for the optimization of advantageous diffusion effects, and new procedures for biomass recovery.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260210206
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  • 6
    Electronic Resource
    Electronic Resource
    Penicillin G production by immobilized whole cells of Penicillium chrysogenum (1979)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 21 (1979), S. 261-270 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Penicillium chrysogenum was immobilized in polyacrylamide gel prepared from 5% acrylamide monomers (85% acrylamide and 15% N,N′-methylene bisacrylamide). Penicillin produced from glucose by the immobilized mycelium was 17% of that produced by washed mycelium. However, the activity of penicillin production of the washed mycelium decreased with repeated use. On the other hand, the activity of the immobilized mycelium increased initially and decreased gradually with repeated use. The rate of oxygen uptake of the immobilized mycelium was about 30% of that of the washed mycelium. The immobilized mycelium required oxygen for the production of penicillin.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260210211
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  • 7
    Electronic Resource
    Electronic Resource
    High-resolution flow-zonal centrifuge system (1979)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 21 (1979), S. 317-321 
    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: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260210215
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  • 8
    Electronic Resource
    Electronic Resource
    Microbial growth on hydrocarbons: Role of flocs (1979)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 21 (1979), S. 337-339 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260210219
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  • 9
    Electronic Resource
    Electronic Resource
    Improved nonporous magnetic supports for immobilized enzymes (1979)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 21 (1979), S. 393-416 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Ni powders coated by deposition of TiO2 or controlled oxidation to NiO develop substantial resistance to corrosion. Chymotrypsin immobilized to these coated Ni supports shows very high stability of activity on storage. Chymotrypsin immobilized by adsorption and glutaraldehyde crosslinking was fairly rapidly eluted under operational conditions in the presence of substrate. If 3-aminopropyltriethoxysilane (APS) was used to produce a covalent linkage, desorption of enzyme still occurred because of relatively unstable bonding of the silane to the oxide surface. A more stable attachment was produced by joining together many silane links with a layer of polyglutaraldehyde. The mechanism of action of APS as a coupling agent under these conditions is discussed. γ-Fe2O3, and particularly a Mn-Zn ferrite, are suitable magnetic support materials available with smaller particle sizes. Particles below 1 μm give the expected higher specific activities of immobilized enzymes.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260210304
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  • 10
    Electronic Resource
    Electronic Resource
    Immobilization of enzymes on activated carbon: Selection and preparation of the carbon support (1979)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 21 (1979), S. 461-476 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Based upon its superior catalytic activity for H2O2 decomposition, a bituminous coal-based activated carbon was selected for investigations of pretreatment and enzyme immobilization methods. Pretreatments considered include acid washing, exposure to strong oxidizing agents, contact with concentrated peroxide solutions, nitration and amination, isothiocyanate derivatization, silanization, and stearic acid coating. Effects of these pretreatments on morphology and trace-metal content of the carbon pellets have been studied using scanning electron microscopy and dispersive analysis of x rays. Immobilization of glucoamylase by adsorption, glutaraldehyde crosslinking, and covalent attachment to carbon activated by water-soluble diimide or diazotization have been examined. These different enzyme-carbon catalysts have been characterized by their enzyme loading, enzyme activity, catalytic activity for H2O2 decomposition, or combinations of these measures of performance.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260210308
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