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  • Biochemistry and Biotechnology  (6)
  • Wiley-Blackwell  (6)
  • Wiley
  • 1990-1994  (4)
  • 1985-1989  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Lipolytic activities of a lipase immobilized on six selected supporting materials (1990)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 35 (1990), S. 132-137 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Six different types of materials including PVC, chitosan, chitin, agarose, Sepharose, and Trisacryl were evaluated for their lipase-coupling efficiencies. Among those tested, chitosan yielded the highest amount of lipase (79 mg/mL packed gel) immobilized but with lowest oil hydrolytic activity (0.03 mg eq/mL gel). The amount of lipase immobilized was affected by the length of the hydrocarbon chain attached to the PVC matrix but not by the pore size of the supports used. On the other hand, the specific activity of the immobilized lipase was affected by the pore size but not by the chain length of the hydrocarbon attached to the support. After immobilization, the optimal reaction pH was shifted from 7.5 to 8.5 and the optimal reaction temperature from 35 to 45-55°C. Lipase immobilized on PVC exhibited higher thermal stability than that on agarose. The half-life of the PVC immobilized lipase operating at 30°C in a packed-bed reactor was estimated to be about 400 h.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260350204
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  • 2
    Electronic Resource
    Electronic Resource
    Changes of lipase-catalyzed lipolytic rates in a batch reactor (1992)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 39 (1992), S. 1128-1132 
    Details
    ISSN: 0006-3592
    Keywords: lipolytic rates ; hydrolysis ; tributyrin ; Candida rugosa ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A dramatic change of the reaction rate was observed for the lipase-catalyzed hyrolysis of tributyrin in a batch reactor. Immediately after the addition of the enzyme, the lipolysis rate increased continuously until a maximal reaction rate was reached. The duration of the induction was mainly controlled by the bulk enzyme concentration and the reactor stirring speed. The reaction rate dropped sharply after reaching its maximal value. The lipolysis decayed at a rate of about 0.012 min-1, and was not affected by changes of the stirring speed. This decay was attributed to the fast deactivation of the surface-adsorbed lipase, and possibly to the extremely slow desorption of the inactivated species. For reaction time longer than 120 minutes, the lipolysis decreased at a much slower rate. Several mechanisms for the decay of the lipolysis rate were discussed.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260391108
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  • 3
    Electronic Resource
    Electronic Resource
    Preparation of various glucose esters via lipase-catalyzed hydrolysis of glucose pentaacetate (1987)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 29 (1987), S. 648-651 
    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-D(+)-Glucose pentaacetate was hydrolyzed both chemically and enzymatically. In contrast to the alkaline hydrolysis, esterase-catalyzed deacetylations afforded significant accumulation of intermediate glucose esters at different degrees of substrate conversion. Aspergillus niger lipase, the most suitable of the four enzymes tested, was used for preparative hydrolysis of glucose pentaacetate. As a result, gram quantities of pure glucose-2,3,4,6-tetraacetate, glucose triacetate (a mixture of two positional isomers, 2,4,6- and 3,4,6-), and glucose-4,6-diacetate were prepared.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260290515
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  • 4
    Electronic Resource
    Electronic Resource
    Measurement of hydrodynamic shear by using a dissolved oxygen probe (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 41 (1993), S. 296-302 
    Details
    ISSN: 0006-3592
    Keywords: shear measurement ; cell culture reactors ; dissolved oxygen probe ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: When a dissolved oxygen (DO) probe is submerged in an air-saturated cell culture medium the thickness of the liquid film that exists outside the membrane of a DO probe changes with hydrodynamic shear. The response of the DO probe thus varies with the hydrodynamic shear environment near the DO probe in cell culture reactors. The thickness of the liquid film was estimated by using a three-layer model, which describes the flow of DO molecules through the liquid layer, the membrane, and the electrolyte, to the cathode of a DO probe. According to the three-layer model, the current output of the DO probe was a strong function of thickness of the liquid film outside the membrane of the DO probe. A correlation between shear rates on the surface of the probe and the DO saturation reading was obtained by using two concentric cylinders with a rotating inner cylinder. This correlation was then used to characterize the local hydrodynamic shear environment in a cell culture reactor. © 1993 John Wiley & Sons, Inc.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260410303
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  • 5
    Electronic Resource
    Electronic Resource
    Lipase-catalyzed oil hydrolysis in the absence of added emulsifier (1988)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 31 (1988), S. 628-633 
    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: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260310618
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  • 6
    Electronic Resource
    Electronic Resource
    Dissociation and electrophoretic separation of dextranase and dextranase inhibitor from a tighly bound enzymeinhibitor complex of Streptococcus sobrinus (1993)
    Weinheim : Wiley-Blackwell
    Electrophoresis 14 (1993), S. 613-618 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Endodextranase was separated from dextranase inhibitor in culture filtrates of Streptococcus sobrinus by sodium dodecyl sulphate-polylamide gel electrophoresis (SDS-PAGE) in gel slabs containing blue dextran. Sample preparation included dissociation of the enzyme from its inhibitor by boiling for 1 min in SDS. During subsequent incubation of the gel, dextranase was located as clear bands on a blue background, and dextranase inhibitor appeared as blue zones on a clear background following incubation in dextranase solution. The enzyme and the inhibitor existed in multiple forms, and the range of molecular masses for dextranase (223-132 kDa) permitted an excellent separation from dextranase inhibitor (49-25 kDa). Although dextranase-negative mutants, and wild type strains grown at low dilution rate in the chemostat, were devoid of free dextranase activity, the enzyme was easily located by analytical SDS-PAGE. Likewise, analysis of filtrates from wild type strains, which contained no free inhibitor activity when growth occurred at high dilution rate, revealed dextranase inhibitor activity on the gels. The total production (free + combined) of dextranase and inhibitor by S. sobrinus was determined by dissociation of enzyme-inhibitor complexes in concentrated cell-free filtrates, their separation by preparative SDS-PAGE and electroelution from the gels, followed by renaturation of protein activity. From a comparison of activity tests of free dextranase and free inhibitor in untreated filtrates with the results of similar tests on renatured electroeluates, the proportion of each constituent bound into a complex under each growth condition could be deduced.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150140196
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