Immobilization of
            <i>Escherichia coli</i>
            Cells Containing Aspartase Activity with Polyurethane and Its Application for
            <scp>l</scp>
            -Aspartic Acid Production

Fusee, Murray C.; Swann, Wayne E.; Calton, Gary J.

doi:10.1128/aem.42.4.672-676.1981

Cited by 48 publications

(4 citation statements)

References 9 publications

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“…Some researchers have assumed that covalent bonds are formed between the polyurethane polymer and the cell surface during immobilization (8). Electron microscopy of Escherichia coli immobilized in polyurethane suggested that the cells were attached to the solid structure of the matrix (10).…”

Section: Mineralization Of Pcp To Co2 By Polyurethane-entrappedmentioning

confidence: 99%

Degradation of pentachlorophenol by polyurethane-immobilized Flavobacterium cells

O’Reilly

Crawford

1989

Appl Environ Microbiol

121

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Polyurethane-immobilized Flavobacterium cells (ATCC 39723) degraded pentachlorophenol (PCP) at initial concentrations as high as 300 mg liter-'. The reversible binding of PCP to the polyurethane was shown to be important in the protection of the cells from inhibition of PCP degradation. The degradation activity of the bacteria was monitored for 150 days in semicontinuous batch reactors. The degradation rate dropped by about 0.6% per day. PCP was degraded in a continuous-culture bioreactor at a rate of 3.5 to 4 mg g of foam-1 day-' for 25 days. Electron micrographs of the polyurethane suggested that the cells were entrapped within 50to 500-,um-diameter pockets in the foam.

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Section: Mineralization Of Pcp To Co2 By Polyurethane-entrappedmentioning

confidence: 99%

Degradation of pentachlorophenol by polyurethane-immobilized Flavobacterium cells

O’Reilly

Crawford

1989

Appl Environ Microbiol

121

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“…As a result, L-aspartic acid production on an industrial scale using Escherichia coli cells immobilized in polyacrylamide was developed in 1973 (Chibata et al, 1974). Subsequently, various other polymers for this process have been proposed and applied (Chibata et al, 1985, Fusee et al,1981; however, it is obvious that continuous improvement of both the biological agents and process technology is necessary. We have previously described our investigations on strain improvement (Gadomska et al, 2007;Papierz et al, 2007) and in this paper, we present our own immobilization method of whole E. coli cells in chitosan for L-aspartic acid biosynthesis in continuous process in column bioreactors.…”

Section: Introductionmentioning

confidence: 99%

Immobilized Cells of Recombinant Escherichia coli Strain for Continuous Production of L-aspartic Acid

Szymańska

Sobierajski²,

Chmiel³

2011

Pol J Microbiol

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For L-aspartic acid biosynthesis, high production cells of Escherichia coli mutant B-715 and P1 were immobilized in chitosan gel using a technique developed in our laboratory. The immobilization process reduced initial activity of the intact cells, however, the biocatalyst produced was very stabile for long-term use in multi-repeated batch or continuous processes. Temperature influence on the conversion of ammonium fumarate to L-aspartic acid was investigated. In long-term experiments, over 603 hours, the temperature 40 degrees C was found to be the best for both biocatalyst stability and high conversion rate. The optimum substrate concentration was 1.0 M. Continuous production of L-aspartic acid was investigated in three types of column bioreactors characterized by different volumes as well as different high to biocatalyst bed volume rations (Hz/Vz). The highest conversion rate, 99.8%, and the productivity 6 g/g/h (mass of L-aspartic acid per dry mass of cells in biocatalyst per time unit) was achieved in the bioreactor with the highest value Hz/Vz = 3.1, and liquid hour space velocity value of 5.2, defined as the volume of feeding substrate passed per volume of catalyst in bioreactor per one hour.

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“…It indeed offers a simple and practicable method for enzyme immobilization and has potential for practical applications in various bioreactors. mers, [9][10][11][12]16,22,23,26,30…”

Section: Introductionmentioning

confidence: 99%

Kinetic studies on urea hydrolysis by immobilized urease in a batch squeezer and flow reactor

Huang

Chen

1992

Biotech & Bioengineering

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The immobilization of urease on the reticulated polyurethane foam, and the kinetic phenomenon of urea hydrolysis by the resulting immobilized urease in both batch squeezer and circulated flow reactors were studied. Urease was immobilized with bovine serum albumin and glutaraldehyde on polyurethane foam support of 7 to 15 mum thickness. The residual apparent activity of urease after immobilization was about 50%. The good hydrodynamic property and flexibility of polyurethane foam were retained in solution after immobilization. A modified biofilm reactor model was used to describe the kinetic phenomenon of urea hydrolysis in both batch squeezer and circulated flow reactors. The characteristic parameters of the reactor model for both bioreactors were obtained by combining the Rosenbrock optimization method, the Rungs-Kutta method, and the Newton-Raphson method. The best-fit results were in good agreement with the experimental data. This study suggests another application of polyurethane foam in enzyme immobilization and immobilized enzyme reactors, which offers potential for practical applications in various bioreactors.

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Immobilization of Escherichia coli Cells Containing Aspartase Activity with Polyurethane and Its Application for l -Aspartic Acid Production

Cited by 48 publications

References 9 publications

Degradation of pentachlorophenol by polyurethane-immobilized Flavobacterium cells

Degradation of pentachlorophenol by polyurethane-immobilized Flavobacterium cells

Immobilized Cells of Recombinant Escherichia coli Strain for Continuous Production of L-aspartic Acid

Kinetic studies on urea hydrolysis by immobilized urease in a batch squeezer and flow reactor

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