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  • 1
    Electronic Resource
    Electronic Resource
    Estimation of parameters in population models for Schizosaccharomyces pombe from chemostat data (1972)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 14 (1972), S. 915-938 
    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 integro-differential growth model of Eakman, Fredriekson, and Tsuehiya has been employed to fit cell size distribution data for Schizosaccharomyces pombe grown in a chemostat under severe product inhibition by ethanol. The distributions were obtained with a Coulter aperture and an electronic system patterned after that of Harvey and Marr. Four parameters - mean cell division size, cell division size standard deviation, daughter cell size standard deviation, and a growth rate coefficient - were calculated for models where the cell growth rate was inversely proportional to size, constant, and proportional to size. A fourth model, one where sigmoidal growth behavior was simulated by two linear growth segments, was also investigated. Linear and sigmoidal models fit the distribution data best. While the mean cell division size remained relatively constant at all growth rates, standard deviation of division size distribution increased with increasing holding times. Standard deviation of the daughter size distribution remained small at all dilution rates. Unlike previous findings with other organisms, the average cell size of Schizosaccharomyces pobme increased at low growth rates.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260140605
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  • 2
    Electronic Resource
    Electronic Resource
    Properties of ribulose diphosphate carboxylase immobilized on porous glass (1974)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 16 (1974), S. 1507-1516 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Ribulose-1,5-diphosphate carboxylase from spinach has been bound to arylamine porous glass with a diazo linkage and to alklamine porous glass with glutaraldehyde. Stability at elevated temperatures and responses to changes of pH and ribulose-1,5-diphosphate, Mg2+, and dithiothreitol concentrations were not significantly different from the soluble enzyme, though stability at 4°C was somewhat improved.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260161107
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  • 3
    Electronic Resource
    Electronic Resource
    Pilot plant production of glucose with glucoamylase immobilized to porous silica (1976)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 18 (1976), S. 253-267 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Glucoamylase was immobilized to porous silica and its kinetics and stability were observed with acid- and α-amylase-hydrolyzed dextrin as feed. The enzyme was found to be extremely stable in both laboratory and pilot plant operations. When the feed had been previously only lightly hydrolyzed, pore diffusion limitation caused appreciable decreases in glucose production rate. The severity of starch hydrolysis to dextrin markedly affected ultimate glucose yields. The diffusional gradients present in the carrier pores caused the immobilized enzyme to yield lower glucose concentrations than the free enzyme at similar feed conditions.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260180210
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  • 4
    Electronic Resource
    Electronic Resource
    Immobilization and characterization of hog kidney mutarotase (1977)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 19 (1977), S. 923-928 
    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.260190610
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  • 5
    Electronic Resource
    Electronic Resource
    Experimental operation of immobilized multienzyme systems in optimal and suboptimal configurations (1978)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 20 (1978), S. 243-253 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Two mixed immobilized enzyme systems, glucoamylase-glucose isomerase and glucose isomerase-glucose oxidase-catalase, were operated to verify theoretical predictions that optimal bifunctional catalyst configutations could exist superior to those where the catalysts were mixed uniformly or arranged sequentially in a tubular reactor. The experimental results for all three configurations conformed to the theoretical values sufficiently closely to support of optimal catalyst profiles.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260200207
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  • 6
    Electronic Resource
    Electronic Resource
    Properties of β-amylase immobilized to alkylamine porous silica (1979)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 21 (1979), S. 505-512 
    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: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260210312
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  • 7
    Electronic Resource
    Electronic Resource
    Effect of pore diffusion limitation on dextrin hydrolysis by immobilized glucoamylase (1980)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 22 (1980), S. 1-17 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Data reported here and previously indicate that when dextrin is hydrolyzed in the presence of immobilized glucoamylase, use of a larger average molecular weight substrate leads to lower overall rates of hydrolysis, while the maltose concentration during the bulk of the reaction and the maximum glucose concentration are lower than when the soluble form of the enzyme is employed under the same conditions. Computer simulation of the system demonstrated that all three observations were caused by pore diffusion limitation: the first by slow diffusion of substrate, the second by slow diffusion of intermediates, and the third by slow diffusion of glucose. Follow-up experiments with glucoamylase immobilized to particles of different sizes confirmed this finding, as results with the smallest beads were identical to those with soluble glucoamylase.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260220102
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  • 8
    Electronic Resource
    Electronic Resource
    Immobilization and properties of Leuconostoc mesenteroids dextransucrase (1980)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 22 (1980), S. 1055-1069 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Dextransucrase from Leuconostoc mesenteroides (NRRL B-512F) was purified by ultrafiltration and gel filtration chromatography in 54% yield. The specific activity of a heart cut was 58.6 U/mg; cumulative purification of that preparation was 247-fold. Of 13 carriers surveyed, only alkylamine porous silica gave immobilization efficiencies consistently above 15 %. Immobilization to silica changed the properties of dextransucrase relatively little, the optimum pH for activity remaining at 5.2, while that for stability decreased from pH 5.5-6 to pH 5.2. In short assays, highest activities of both soluble and immobilized dextransucrase occurred at 30°C. Activation energies below that temperature were 8.6 kcal/mol for the former form and 1.7 kcal/mol for the latter. Maximum stabilization of soluble dextransucrase was attained by 5mM Ca2+.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260220513
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  • 9
    Electronic Resource
    Electronic Resource
    Properties of soluble and immobilized Aspergillus niger β-xylosidase (1980)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 22 (1980), S. 1143-1154 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Aspergillus niger β-xylosidase was characterized when in soluble form and when immobilized to alkylamine porous silica with glutaraldehyde and to alumina with titanium tetrachloride. Energies of activation averaged 13.4 KcaL/mol for the soluble enzyme, 9.0 Kcal/mol when immobilized to alumina, and 8.0 Kcal/mol when bound to silica. The highest activity of all forms of β-xylosidase was found near pH 3. The soluble enzyme was highly stable at pH 4, where lowest rates of decay occurred, and temperature of 65°C and below. The decay rates of alumina-bound β-xylosidase and pH 4 and equivalent temperatures were approximately 10 times as high. Michaells constants were 0.200 and 0.262mM for o-nitrophenyl-β-D-xylopyranoside with soluble and alumina-bound β-xylosidase, respectively.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260220604
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  • 10
    Electronic Resource
    Electronic Resource
    Purification and immobilization of Aspergillus niger β-xylosidase (1980)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 22 (1980), S. 1127-1142 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: β-Xylosidase from a commercial Aspergillus niger preparation was purified by differential ammonium sulfate precipitation and either gel permeation or cation exchange chromatography, giving 16-fold purification in 32% yield for the first technique or 27-fold purification in 19% yield for the second. The second method in addition almost completely removed interfering β-glucosidase activity. Enzymes prepared by this method was immobilized to 10 different carriers, but only when it was bound to alumina with TiCl4 and to alkylamine porous silica with glutaraldehyde were substantial efficiencies and stabilities achieved. With alumina, the variation of activation procedure, amount of β-xylosidase offered, and activation solution composition yielded maximum activities of over 40 U/g with approximately 70% immobilization efficiency. Variation of binding pH and incubation time led to a maximum immobilized activity of 1.3 U/g with 78% immobilization efficiency on silica.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260220603
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