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  • Analytical Chemistry and Spectroscopy  (4,318)
  • ASTROPHYSICS  (2,970)
  • Biochemistry and Biotechnology  (1,710)
  • 1980-1984  (8,998)
Collection
Keywords
Publisher
Years
Year
  • 1
    Electronic Resource
    Electronic Resource
    Large-scale preparation of a lectin from sunn hemp seeds (Crotalaria juncea) (1980)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 22 (1980), S. 79-88 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A procedure for large-scale preparation of a lectin from Crotalaria juncea seeds is described. The method involve fractionation by pH- and ammonium sulfate precipitation followed by biospecific affinity chromatography. The adsorbent used for the affinity chromatography was prepared by coupling galactose to Sepharose 6B activated with divinylsulfone. A comparison of different apparatus and techniques involved in the preparation is discussed. The yield and quality of the lectin prepared at a large scale were comparable with laboratory-scale preparation. From 50 kg Crotalaria juncea beans, 14.4 g Crotalaria lectin were obtained.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260220107
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  • 2
    Electronic Resource
    Electronic Resource
    Model of growth and ergot alkaloid production by Claviceps purpurea (1980)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 22 (1980), S. 255-270 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A growth model for Claviceps purpurea in submerged batch culture is presented. In developing the model, the basic principles of the growth and the morphological properties of C. purpurea are considered. The growth of C. purpurea is assumed to occur in a three-step manner; the first step involves the assimilation and the growth of cells; the second one involves cell division, and the third one involves transformation of the mature cells to a state where they have no ability to divide but do have the ability to produce ergot alkaloids and then they gradually die. Inorganic phosphate is assumed to be the limiting substrate for the first and the second steps in conditions of carbon source being in excess. The model constants are determined by model simulation and graphical searching techniques to find the minimum value of the absolute difference between the experimental and the simulated curves for biomass, alkaloids, and sucrose.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260220202
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  • 3
    Electronic Resource
    Electronic Resource
    Immobilization of β-galactosidase and other enzymes onto p-amino-carbanilated cellulose derivatives (1980)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 22 (1980), S. 311-321 
    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-Galactosidase and other enzymes were immobilized on p-amino-carbanilated derivatives of cellulose and methylol cellulose using the diazo method and through glutaraldehyde. The optimum conditions for coupling cellulose tri-(p-amino-carbanilate) (CTAC) to β-galactosidase were established. The diazo coupling method with CTAC gave greater activity than with glutaraldehyde when coupled to β-galactosidase (Escherichia coli). The stability of the CTAC-β-galactosidase system was examined. The disubstituted p-amino-carbanilate derivative (CDAC) gave a lower activity, whereas the methylol analog (MCTAC) gave slightly greater activity. The CTAC was also used to immobilize glucose oxidase, trypsin, pepsin, and papain.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260220206
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  • 4
    Electronic Resource
    Electronic Resource
    Hydrophobic chromatography of β-galactosidase (1980)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 22 (1980), S. 377-399 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The hydrophobic interaction of β-galactosidase with Sepharose 4B substituted with 3,3′-diaminodipropylamine was studied in both batch and column experiments. The equilibrium and the binding rate constants were determined for different phosphate buffer concentrations. The equilibrium constants exhibit a hysteresis effect, i.e., desorption constants are less than adsorption constants, and the higher the ionic strength to start the desorption, the larger the effect. The rate data are not satisfactorily described by a simple reversible first-order model. The column chromatographic data are semiquantitatively described by a local equilibrium theory without axial dispersion or intraparticle diffusion.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260220211
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  • 5
    Electronic Resource
    Electronic Resource
    Enzyme formation during solid-substrate fermentation in rotating vessels (1980)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 22 (1980), S. 411-420 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Aspergillus awamori NRRL 4869 was cultured on the solid substrate, wheat bran, in a modified Rollacell apparatus to produce α-galactosidase and invertase. The swivel cap on the elongated bottle permits the introduction of air while the bottle rotates. Parameters of air flow rate (0.05-0.2 liter/kg/min), rpm (0.15-15 rpm), and weight of solids (150 and 300 g) were varied. At low air flow rates (0.05 liter/kg solid/min), α-galactosidase production was minimal independent of the rotation rate. At 0.15 rpm and 0.2 liter/kg solids/min air flow rate, invertase production ceased after five days; whereas α-galactosidase production continued. The modified Rollacell can be a useful apparatus for studying solid-substrate cultures.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260220213
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  • 6
    Electronic Resource
    Electronic Resource
    Temperature and pH dependence of mold α-galactosidase (1980)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 22 (1980), S. 505-518 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The effect of temperature and pH on kinetic behavior of α-galactosidase of Mortierella vinacea was investigated on the hydrolysis of p-nitrophenyl-α-D-galactopyranoside (PNPG). A very unusual kinetic behavior was observed for the soluble α-galactosidase i.e., substrate inhibition diminished gradually with increasing temperature or near the neutral pH range, and the kinetics approached the ordinary Michaelis-Menten (MM) type. On the other hand, with decreasing temperature or in acidic pH range, substrate inhibition was accelerated. Therefore, Arrhenius plots based on the initial reaction rate did not give straight lines. Furthermore, the slope in the Arrhenius plot changed with substrate concentration, which would make the determination of a characteristic value using conventional methods meaningless. However, the Arrhenius plots of individual kinetic parameters in the rate equation resulted in straight lines in the temperature range 15 to 50°C. From this, the drastic change in kinetic behavior could be explained in connection with the temperature and pH dependence of kinetic parameters in the model. For mold pellets (whole-cell enzyme), however, the influence of temperature and pH was less apparent than that of soluble enzyme because of the limitation in intraparticle diffusion. By using the rate equation that was determined for soluble enzyme and the theoretically derived effectiveness factor, the overall reaction rate for mold pellets at various temperature and pH could be predicted to some extent.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260220304
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  • 7
    Electronic Resource
    Electronic Resource
    Optimization of the production of progesterone 11α-hydroxylase by Rhizopus nigricans (1980)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 22 (1980), S. 555-570 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The progesterone 11α-hydroxylase of Rhizopus nigricans ATCC 6227b is an inducible enzyme system that is primarily induced by its substrate progesterone. Maximum induction was found at a progesterone concentration of 0.5 g/liter or above. Oxygen is the other substrate for the hydroxylation and this was found to have a major effect on the amounts of hydroxylase synthesized. Optimum induction of the hydroxylase in a fermentation with a 3.1 m/sec impeller tip speed was found to occur at a dissolved oxygen tension (DOT) of 10% of air saturation. The agitation rate also effects the amount of hydroxylase synthesized with an apparent maximum at 3.1 m/sec impeller tip speed. The DOT for a maximum hydroxylation rate was much higher than for enzyme synthesis so that it was preferable to increase the DOT after induction was completed.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260220308
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  • 8
    Electronic Resource
    Electronic Resource
    Growth of yeast on n-alkanes. II. Batch experiments (1980)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 22 (1980), S. 615-637 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: In this paper the results of the Monte Carlo simulations as described in an earlier paper are compared with those of batch experiments. A number of batch experiments were carried out at a low inoculation rate so that only a fraction of the oil drops were inoculated. Under these conditions the effect of the segregation of the oil phase is more clearly demonstrated. Special attention is paid to the preparation of actively growing yeast cells with which the cultures is inoculated. Also a method is developed to estimate the amount of actively growing cells with which the culture is inoculated. The other parameters necessary for the Monte Carlo simulation are measured in separate experiments: the maximum growth rate of the cells, oil drop size, and the drop parameters. Finally the growth curves (measured in the batch experiments) are compared with those calculated with the Monte Carlo procedure. A good agreement is found.
    Additional Material: 17 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260220311
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  • 9
    Electronic Resource
    Electronic Resource
    Mechanism of the enzymatic hydrolysis of cellulose: Effects of major structural features of cellulose on enzymatic hydrolysis (1980)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 22 (1980), S. 177-199 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The susceptibility of cellulose to enzymatic hydrolysis is affected by the structural features of cellulosic materials. It has been suggested that the crystallinity and surface area of cellulose fibers are the most important structural features in this regard. This study investigated in depth the relative effects of these two structural features upon the enzymatic hydrolysis of cellulose and the change of the structural parameters of cellulose during the course of hydrolysis. It was found that the hydrolysis rate is mainly dependent upon the fine structural order of cellulose which can best be represented by the crystallinity rather than the simple surface area. Monitoring the changes in the structural parameters during the course of reaction showed that surface area is not a major limiting factor that slows hydrolysis in its late stages as has been suggested. This information concerning structural features is used to elucidate the mode of action of cellulase.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260220113
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  • 10
    Electronic Resource
    Electronic Resource
    Simple device for the spectrophotometric assay of immobilized enzymesThis work was presented at the September 30, 1977 meeting of the New Mexico Academy of Science at Silver City, New Mexico. (1980)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 22 (1980), S. 227-229 
    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: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260220117
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