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  • 1
    Electronic Resource
    Electronic Resource
    Studies on the production and application of cellulase from Trichoderma reesei QM-9414 (2000)
    Springer
    Bioprocess engineering 22 (2000), S. 467-470 
    Details
    ISSN: 0178-515X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract  High yielding mutant strain, Trichoderma reesei QM-9414, was employed for the cellulase enzyme production. Enzyme production conditions (pH, inoculum age and concentration, and organic supplements) were optimized. The ability of partially purified enzyme to hydrolyze various regionally abundant lignocellulosic raw materials was studied. Enzymatic hydrolysis conditions (temperature, pH, enzyme and substrate concentrations) were optimized. Temperature 50 °C, pH 4.5, enzyme concentration 40 FPU/g substrate and substrate concentration 2.5% were found to be optimum for the maximum yields of sugars. β-glucosidase supplementation was found to increase both the sugar yield and hydrolysis rate, and shorten the reaction time significantly.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004490050760
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Response Surface Modeling of Lipase-Catalyzed Isoamyl Propionate Synthesis (2002)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 67 (2002), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: : Response surface methodology based on a 3-variable, 5-level central composite rotatable design matrix was used to optimize the synthesis. The influence of selected variables, namely, enzyme/substrate (E/S) ratio, substrate concentration, and temperature was investigated. E/S ratio and temperature had a strong effect on esterification, while substrate concentration did not. Reaction time did not show significant effect on ester yields, and conversions could be completed in less than 24 h. The response surface model has been found to describe the experimental results adequately. Product yield at optimum conditions (24 g/mol E/S ratio, 1.5 M substrate concentration 20 °C) was 1.4 M, representing 93% conversion, which is in good agreement with the predicted one.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.2002.tb11354.x
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  • 3
    Electronic Resource
    Electronic Resource
    Enzymatic synthesis of isoamyl butyrate using immobilized Rhizomucor miehei lipase in non-aqueous media (2000)
    Springer
    Journal of industrial microbiology and biotechnology 25 (2000), S. 147-154 
    Details
    ISSN: 1476-5535
    Keywords: Keywords: enzymatic synthesis; esterification; flavor ester; isoamyl butyrate; lipase; solvent-free synthesis; Rhizomucor miehei
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Isoamyl butyrate, an important fruity flavor ester, was synthesized using Rhizomucor miehei lipase immobilized on a weak anion exchange resin (Lipozyme IM-20) by the esterification of isoamyl alcohol and butyric acid. The effects of various reaction parameters such as substrate and enzyme concentrations, substrate molar ratio, temperature and incubation time have been investigated. Yields above 90% were obtained with substrate concentrations as high as 2.0 M. No evidence of enzyme inhibition by butyric acid was present up to 1.0 M concentration. Acid inhibition and, to a small extent, alcohol inhibition were evident above 1.0 M substrate concentration. Conversions reached a saturation value by the end of 24–48 h of incubation due to the accumulation of the water of reaction. The equilibrium was successfully pushed forward towards esterification by removing the accumulated water using a molecular sieve.Journal of Industrial Microbiology & Biotechnology (2000) 25, 147–154.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/sj.jim.7000045
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  • 4
    Electronic Resource
    Electronic Resource
    Optimization of enzymatic hydrolysis of mango kernel starch by response surface methodology (2000)
    Springer
    Bioprocess engineering 23 (2000), S. 681-685 
    Details
    ISSN: 0178-515X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract  Amyloglucosidase (EC 3.2.1.3) from Aspergillus niger was employed for the saccharification of mango (Mangifera indica Linn) kernel starch. Response surface methodology based on a three-level three-factor Box–Behnken design was employed to optimize the important process variables such as substrate concentration (137.5–412.5 mg), enzyme concentration (4–12 mg) and temperature (35–55 °C). The sugar yield increased with both enzyme concentration and temperature, and decreased with substrate concentration. The response surface model indicated optimum conditions (substrate, 137.5 mg; enzyme, 12 mg; temperature, 55 °C) for obtaining 0.4851 mg sugar/mg substrate, which was also verified experimentally.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004490000220
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  • 5
    Electronic Resource
    Electronic Resource
    An esterification method for determination of lipase activity (2000)
    Springer
    Biotechnology letters 22 (2000), S. 1511-1514 
    Details
    ISSN: 1573-6776
    Keywords: butyl butyrate ; butyric acid ; esterification ; lipase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract The choice of a lipase for an esterification reaction can be determined from the esterification reaction between butyric acid (0.16 M) and butanol (0.33 M) at 50 °C and agitated with 10 mg lipase. The decrease in butyric acid is measured by titration and 1 unit of lipase activity is defined as 1 μmol butyric acid consumed per min per mg lipase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1005604206258
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    Paper (German National Licenses)
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