Immobilized enzymes in organic media: Determinants of water dependence. Interim report

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Description

The overall goals of our DOE-funded project are to investigate the critical factors that limit commercial scale applications of enzymes in organic solvents, and to scale-up a process for the production of a precursor to optically active polymers. Initially, we are attempting to quantify the effect of intra-particle dynamics on overall process performance. This involves examination of coupled enzyme kinetics, solubility, wetting and mass transfer effects toward support selection, reactor design/scheme and scale-up. For this study we selected a pure enzyme preparation: a lipase from C. Viscosum. The enzyme has been immobilized on celite and the catalyzed interesterification kinetics in ... continued below

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22 p.

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Nandi, S.; DeFilippi, I.; Bedwell, B. & Zemel, H. June 1, 1993.

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Description

The overall goals of our DOE-funded project are to investigate the critical factors that limit commercial scale applications of enzymes in organic solvents, and to scale-up a process for the production of a precursor to optically active polymers. Initially, we are attempting to quantify the effect of intra-particle dynamics on overall process performance. This involves examination of coupled enzyme kinetics, solubility, wetting and mass transfer effects toward support selection, reactor design/scheme and scale-up. For this study we selected a pure enzyme preparation: a lipase from C. Viscosum. The enzyme has been immobilized on celite and the catalyzed interesterification kinetics in petroleum ether and its dependence on water concentration have been determined. The results are very similar to those obtained in the past with crude Pseudomonas Cepacia. So far we have formulated a model for tripalmitin depletion, based on taking mass balances. A parameter has been included which accounts for the effect of water content inside the celite particle. The initial rate of depletion can be described by Monod-like kinetics. Our experimental data, at 0.003 mg H{sub 2}O per cm{sup 2}, fit a model and parameters presented in the literature. Because of the small size of the support, the relatively low amount of water, and the low reaction rates, our calculations predict that the lipase system at 0.003-0.01 mgH{sub 2}O/cm{sup 2} is reaction rate limited. The mass transfer through the organic phase within the support particles is not limiting. In order to test the dense particles with varying diameter but the same total surface area have been tested and compared to the porous celite.

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22 p.

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OSTI as DE97007747

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  • Other Information: PBD: Jun 1993

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  • Other: DE97007747
  • Report No.: DOE/CH/10519--T2
  • Grant Number: FG36-92CH10519
  • DOI: 10.2172/503531 | External Link
  • Office of Scientific & Technical Information Report Number: 503531
  • Archival Resource Key: ark:/67531/metadc691656

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  • June 1, 1993

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  • Aug. 14, 2015, 8:43 a.m.

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  • Nov. 13, 2015, 8:30 p.m.

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Nandi, S.; DeFilippi, I.; Bedwell, B. & Zemel, H. Immobilized enzymes in organic media: Determinants of water dependence. Interim report, report, June 1, 1993; United States. (digital.library.unt.edu/ark:/67531/metadc691656/: accessed September 19, 2017), University of North Texas Libraries, Digital Library, digital.library.unt.edu; crediting UNT Libraries Government Documents Department.