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  • Biochemistry and Biotechnology  (3)
  • Chemical Engineering  (3)
  • 1985-1989  (6)
  • 1950-1954
  • 1
    ISSN: 0032-3888
    Keywords: Chemistry ; Chemical Engineering
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: Thermal and mechanical studies on many linear polyesters have revealed their behavior in crystalline, liquid crystalline, and amorphous phases. Their phase behavior in binary compositions has also been studied by a range of additional techniques and in combinations including the polycarbonate of bisphenol-A. Regions of amorphous compatibility and incompatibility have been identified and measures made of transition temperature changes with composition. The conditions for transreaction have also been determined and the properties measured for the resultant new copolymers.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 32 (1988), S. 669-676 
    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
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  • 3
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 28 (1986), S. 1707-1712 
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Chondroitinase ABC catalyzing the depolymerization of chondroitin sulfate was induced by incubating the Proteus vulgaris cells in a medium containing chondroitin C sulfate as an inducer. Incubation of P. vulgaris cells for 12 h in the presence of 0.3% inducer was optimal to obtain the cells with highly active chondroitinase ABC. Such cells were immobilized in k-carrageenan gel lattice, and some properties of chondroitinase ABC in immobilized cells were studied in comparison with those of the enzyme without immobilization (free enzyme). The stabilities of the enzyme toward heat and storage were remarkably improved by immobilizing the cells in k-carrageenan gel lattice. Optimal pH and temperature for activity of the enzyme were slightly shifted to the alkaline region and higher temperature by immobilization and were 9.0 and 35°C, respectively.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 33 (1989), S. 845-855 
    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
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  • 5
    Electronic Resource
    Electronic Resource
    Hoboken, NJ : Wiley-Blackwell
    AIChE Journal 33 (1987), S. 1522-1532 
    ISSN: 0001-1541
    Keywords: Chemistry ; Chemical Engineering
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The Kinetics of the SO2-Na2CO3 reaction were studied at 353 to 413 K and atmospheric pressure with thermal gravimetric analysis data. Since the reaction is very fast, special precautions were taken to operate at conditions such that transport effects did not influence results. The data indicated that Na2SO3 was formed by two paths: direct reaction, and adsorption of SO2 followed by conversion of adsorbed SO2 to adsorbed CO2 and finally desorption to final product. Rate constants were evaluated for each step in the proposed mechanism. Product distribution predicted from the rate constants agreed well with the distribution calculated from the experimental data at temperatures from 353 to 413 K. At 413 K the results suggested a change in mechanism.
    Additional Material: 18 Ill.
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  • 6
    Electronic Resource
    Electronic Resource
    Hoboken, NJ : Wiley-Blackwell
    AIChE Journal 35 (1989), S. 339-342 
    ISSN: 0001-1541
    Keywords: Chemistry ; Chemical Engineering
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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