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  • Biochemistry and Biotechnology  (231)
  • Wiley-Blackwell  (231)
  • Oxford University Press
  • 2015-2019
  • 1990-1994  (231)
  • 1
    Electronic Resource
    Electronic Resource
    Continuous culture system for production of biopolymer levan using erwinia herbicola (1991)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 38 (1991), S. 557-560 
    Details
    ISSN: 0006-3592
    Keywords: levan ; continuous culture ; molecular weight ; Erwinia herbicola ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The optimal production of the fructan biopolymer levan by the bacterium Erwinia herbicola was investigated, including variations in nitrogen, carbon and phosphorous sources, pH, incubation time, culture yields up to 19% by weight produced based on conversion of sucrose as the carbon source when grown in a continuous culture system and processed by tangential flow filtration. Product identity was confirmed with gas chromatography (GC) and 13C nuclear magnetic resonance (NMR). Gel permeation chromatography (GPC) and low-angle laser light scattering (LALLS) determination of the molecular weight of the product showed a significant difference in molecular weight values dependent on the method of analysis. Analysis by GPC resulted in molecular weight one order of magnitude lower than LALLS independent of sample, underscoring the unusual nature of this biopolymer.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260380515
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  • 2
    Electronic Resource
    Electronic Resource
    Engineering cellulase mixtures by varying the mole fraction of Thermomonospora fusca E5 and E3, Trichoderma reesei CBHI, and Caldocellum saccharolyticum β-glucosidase (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 42 (1993), S. 1019-1028 
    Details
    ISSN: 0006-3592
    Keywords: Caldocellum saccharolyticum ; cellulose ; binding ; β-glucosidase ; hydrolysis ; mole fraction ; synergism ; Thermomonospora fusca ; Trichoderma reesei ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: In this study, different mole fractions of pure Thermomonospora fusca E5 and E3, plus Trichoderma reesei CBHI were studied for reducing sugar production at 2 h, degree of synergism, and cellulose binding. In addition, the effects of introducing the Caldocellum saccharolyticum β-glucosidase into this cellulase system were investigated. The cellulases used were purified to homogeneity. Avicel PH 102 (4% w/w solution in 0.05 sodium acetate pH 5.5 buffer) was the substrate. Reactions were run at 50°C for 2 h using total cellulase concentrations of 8.3 or 12.2 μM. A bimixture of T. fusca E3 and T. reesei CBHI was very effective in hydrolyzing microcrystalline cellulose (9.1% conversion). The addition of endoglucanase E5 to the mixture only increased conversion to 9.8%. However, when both E5 and β-glucosidase were added, conversion increased to 14%. It was also observed that increasing total cellulase concentration beyond 8.3 μM did little to increase percent conversion of cellulose into glucose. The results of the binding studies indicate no competition for binding sites between the endo- and exocellulases. © 1993 John Wiley & Sons, Inc.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260420902
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  • 3
    Electronic Resource
    Electronic Resource
    Determination of total and active immobilized enzyme distribution in porous solid supports (1992)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 39 (1992), S. 679-687 
    Details
    ISSN: 0006-3592
    Keywords: immobilized enzyme distribution ; diffusion cell ; active-site titration ; controlled-pore glass ; cell profile ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The total and active immobilized enzyme (IME) distributions in porous supports are studied both theoretically and experimentally. In order to determine experimentally the enzyme distribution profiles within a single particle, we construct a diffusion cell containing controlled-pore glass particles such that the cell would mimic a large pellet support. Our purpose is to study the interplay between the diffusion process within the interparticle void space and immobilization process in the controlled-pore glass particles onto the evolution of the (total and active) enzyme distributions. A mathematical model is developed to describe the interaction of various processes within the diffusion cell. The immobilized enzymes are determined for a system of trypsin and controlled-pore glass particles. The total amount of enzymes are determined by the amino acid analysis, and the active fraction is obtained by an active-site titration. The experimentally measured total IME profiles compare very well with that predicted by the model. The determined active enzyme profile is found to be nonuniform one, and it represents about 40% of the total enzyme immobilized in the support particles.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260390613
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  • 4
    Electronic Resource
    Electronic Resource
    Gluco-oligosaccharide synthesis by free and immobilized β-glucosidase (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 42 (1993), S. 303-308 
    Details
    ISSN: 0006-3592
    Keywords: gluco-oligosaccharides ; sorbitol ; glucose ; disaccharides ; immobilized enzymes ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Gluco-oligosaccharides were synthesized through the enzymatic condensation of D-glucose at high concentration using a commercial almond β-glucosidase. The synthesis reactions were carried out with both free and immobilized enzyme, with or without sorbitol, an efficient depressor of water activity (aw) in the presence of different glucose concentrations. The yield and the composition of the gluco-oligosaccharides produced changed with the reaction mixture and the form of the enzyme used (free or immobilized). The use of 5 M glucose solution permitted only disaccharides to be obtained, whereas with a glucose concentration of 7.5 M glucose, di-, tri-, and tetrasaccharides were produced. A 7.5 M glucose solution used with 4.4 M sorbitol gave three times more disaccharides than the same solution without sorbitol. Moreover, the immobilized enzyme was much more active in synthesis. The synthesis yield (oligomers mg/mL · mg of enzyme) after immobilization was 573% compared to that of the free enzyme, when a 7.5 M glucose solution was tested. The effects of substrate concentration, sorbitol addition and enzyme immobilization were investigated. © 1993 John Wiley & Sons, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260420306
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  • 5
    Electronic Resource
    Electronic Resource
    Immobilized cell biocatalyst activation and pseudo-steady-state behavior: Model and experiment (1990)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 35 (1990), S. 609-629 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: An intrinsic, unstructured model has been utilized to describethe startup dynamics of a continuous Caalginate-immobilized Zymomonas mobilis (ATCC 10988) fermentation. This model predicts, at least qualitatively, transients in the fermenter effluent glucose, ethanol, and biomass concentrations as well as radial gradients in immobilized-cell concentration and activity within the gelbiocatalysts. Predicted intrabiocatalyst gradients in immobilized-cell specific growth rate were used to calculate the corresponding gradients in intracellular RNA level based on a reported linear relationship between the two. Mathematical simulations of immobilized biomass concentration profiles and RNA content were verified using a novel, scanning microfluorimetry technique.
    Additional Material: 12 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260350608
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  • 6
    Electronic Resource
    Electronic Resource
    Effect of serum concentration on hybridoma viable cell density and production of monoclonal antibodies in cstrs and on shear sensitivity in air-lift loop reactors (1992)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 39 (1992), S. 891-897 
    Details
    ISSN: 0006-3592
    Keywords: air-lift loop reactor ; shear ; serum ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The death rate of hybridoma cells, grown in a continuous culture, has been studied in a small air-lift loop reactor as a function of reactor height and injected gas flow rate. The first-order death-rate constant was found to be proportional to the reciprocal height and to the gas flow rate, in accordance with the hypothetical killing volume model for insect cells in bubble columns. Furthermore, the effect of the serum concentration on viable cell concentration and cell productivity has been investigated in a continuous culture. A serum component became growth limiting when the serum concentration was decreased from 2% to 1%. No effect of the serum concentration on specific cell productivity could be measured. Samples from this culture were also studied in the air-lift loop reactor to determine the effect of serum concentration on the shear sensitivity. The cells' shear sensitivity increased with decreasing serum concentration. The protective effect of serum was found to be physical as well as physiological.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260390902
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  • 7
    Electronic Resource
    Electronic Resource
    Effect of dilution rate on growth, productivity, cell cycle and size, and shear sensitivity of a hybridoma cell in a continuous culture (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 41 (1993), S. 429-439 
    Details
    ISSN: 0006-3592
    Keywords: shear ; air-lift loop reactor ; growth rate ; cell size ; hybridoma cell ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: To study the effects of the growth rate of the hybridoma cell Mn12 on productivity, cell cycle, cell size, and shear sensitivity, six continuous cultures were run at dilution rate of 0.011, 0.021, 0.023, 0.030, 0.042, and 0.058 h-1. This particular hybridoma cell appeared to be unstable in continuous culture with respect to specific productivity, as a sudden drop occurred after about 30 generations in continuous culture, accompanied by the appearance of two populations with respect to the cytoplasmic lgG content. The specific productivity increased with increasing growth rate. The shear sensitivity of the cell, as measured in a small air-lift loop reactor, increased with increasing growth rate. The mean relative cell size, as determined with a flow cytometer, increased with increasing growth rates. Furthermore, the fraction of cells in the S phase increased, and the fraction of cells in the G1/G0 phase decreased with increasing growth rates. © 1993 John Wiley & Sons, Inc.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260410406
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  • 8
    Electronic Resource
    Electronic Resource
    Construction, expression, and analysis of recombinant HIV gp41 constructs containing a novel cellular binding domain (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 42 (1993), S. 81-86 
    Details
    ISSN: 0006-3592
    Keywords: human immunodeficiency virus ; gp41 ; recombinant fusion protein ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The gp41 polypeptide of human immunodeficiency virus (HIV) contains an immunosuppressive domain, an epitope which elicits specific cytolytic T cell responses to HIV, and a complement Clq interactive domain. In addition, a synthetic peptide called CS3, derived from gp41 (amino acids 576-593 of gp160) and contiguous with the major immunodominant domain, binds to cellular proteins and may be important in HIV entry/fusion. In order to further investigate the role of the CS3 region of gp41 in cellular binding and to investigate other properties of gp41, sufficient quantities of this polypeptide must be readily available. We have therefore cloned the region of the HIV genome between nucleotides 7891 and 8188 (corresponding to amino acids 541-639 of gp160) into a series of procaryotic expression vectors. The resulting clones express a recombinant polypeptide of gp41 (r41). Two of these recombinants, pMAL-cRl/r41 and pGEMEX-2/r41, expressed the highest and most consistent levels of r41 as judged by both sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and Western blot analysis. With the pMAL-cRl/r41 construct, r41 was expressed as a fusion to the maltose-binding protein (MBP) and, following purification by affinity chromatography, was cleaved from MBP by factor Xa protease digestion. MBP/r41 may be useful for studies of a reported gp41 cellular binding domain and may facilitate studies involving other functions ascribed to this region of gp41. © 1993 John Wiley & Sons, Inc.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260420111
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  • 9
    Electronic Resource
    Electronic Resource
    Characterization of a recombinant antibody produced in the course of a high yield fed-batch process (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 44 (1994), S. 727-735 
    Details
    ISSN: 0006-3592
    Keywords: monoclonal antibody ; glycosylation ; cell culture ; fed-batch ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Many mammalian cell fed-batch processes rely on maintaining the cells in a viable and productive state for extended periods of time in order to reach high final concentrations of secreted protein. In the work described herein, a nonamplified NSO cell line was transfected with a vector expressing a recombinant human anti-HIV gp 120 monoclonal antibody (Mab) and a selectable marker, glutamine synthetase. A fed-batch process was developed which improved product yields tenfold over the yields reached in batch culture. In this case, the clone was cultured for a period of 22 days and produced 0.85 g Mab/L. To gauge the effect of extended culture lifetime on product quality, biochemical characteristics of MAb isolated from different time points in the fed-batch culture were determined. The apparent molecular weight of the MAb was constant throughout the course of the culture. Isoelectric focusing revealed four major charged species, with a fifth more acidic species appearing later in the culture. The antigen binding kinetics were constant for MAb isolated throughout the culture period. Glycosylation analysis, on the other hand, revealed that MAb produced later in the culture contained greater percentages of truncated N-acetylglucosamine and highmannose N-glycans. Possible contributions to this underglycosylated material from either cell lysis or synthesis from noviable cells were found to be negligible. Instead, the viable cells appeared to be secreting more truncated and high mannose MAb glycoforms as the culture progressed. © 1994 John Wiley & Sons, Inc.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260440609
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  • 10
    Electronic Resource
    Electronic Resource
    The use of hollow fiber cross-flow microfiltration in bioaccumulation and continuous removal of heavy metals from solution by Saccharomyces cerevisiae (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 44 (1994), S. 1362-1366 
    Details
    ISSN: 0006-3592
    Keywords: Saccharomyces cerevisiae ; bioaccumulation ; gel immobilization ; cross-flow microfiltration ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Cross-flow microfiltration was shown to retain Saccharomyces cerevisiae biomass utilized for heavy metal bioaccumulation. The passage of metal-laden influent through a series of sequential bioaccumulation systems allowed for further reductions in the levels of copper, cadmium, and cobalt in the final effluent than that afforded by a single bioaccumulation process. Serial bioaccumulation systems also allowed for partial separation of metals from dual metal influents. More than one elemental metal cation could be accumulated simultaneously and in greater quantities than when a single metal was present in the effluent (Cu2+ 0.43 mmol, Cu2+ + Cd2+ 0.67 mmol, and Cu2+ + Co2+ 0.83 mmol/g yeast dry mass when the initial concentration of each of the metal species was 0.2 mmol·L-1). Co-accumulation of two different metal cations allowed higher total levels of bioaccumulation than found with a single metal. The flux rate was 2.9 × 102 L·h-2μm-2 using a polypropylene microfiltration membrane (0.1 μm pore size) at 25°C. © 1994 John Wiley & Sons, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260441113
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