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  • 11
    Electronic Resource
    Electronic Resource
    Ocimum basilicum seeds as a pellicular support for immobilizing enzymes (1986)
    Springer
    Biotechnology letters 8 (1986), S. 885-888 
    Details
    ISSN: 1573-6776
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary The swollen seeds ofOcimum basilicum consist of a hard core with a pectious porous outer layer to which urease was bound after epoxy activation, through ethylenediamine-glutaraldehyde arm. These seeds can serve as an inexpensive ready to use natural pellicular polysaccharide support for immobilizing enzymes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01078653
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  • 12
    Electronic Resource
    Electronic Resource
    Immobilization of yeast cells by adhesion to glass surface using polyethylenimine (1986)
    Springer
    Biotechnology letters 8 (1986), S. 643-648 
    Details
    ISSN: 1573-6776
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary A method has been described for immobilization of yeast cells by adsorption to glass surface using polyethylenimine for coating cells or glass or both. The immobilized yeast cells were found to be viable and adhered strongly as a monolayer, which could not be desorbed by washing with running tap water or under extreme conditions of pH and ionic strength or during repeated uses in sucrose solutions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01025974
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  • 13
    Electronic Resource
    Electronic Resource
    Effect of permeabilization on the thermostability of catalase in immobilized yeast cells (1987)
    Springer
    Biotechnology letters 9 (1987), S. 625-628 
    Details
    ISSN: 1573-6776
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Catalase in yeast cells is rendered thermolabile on permeabilization using organic solvents or any process of immobilization that eventually permeabilizes the cells. A stable immobilized catalase preparation can be obtained only if yeast cells are immobilized in an intact or viable form.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01033199
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  • 14
    Electronic Resource
    Electronic Resource
    A rapid method for the purification of D-amino acid oxidase of Trigonopsis variabilis by hydrophobic chromatography (1987)
    Springer
    Biotechnology techniques 1 (1987), S. 55-58 
    Details
    ISSN: 1573-6784
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary A relatively simple method has been described for the rapid purification of D-amino acid oxidase from Trigonopsis variabilis by hydrophobic chromatography on Phenyl-Sepharose CL-4B and negative adsorption on DEAE-cellulose. The purified enzyme had a specific activity of 22–24 units at 25°C and exhibited three bands on enzymatic staining.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00156288
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  • 15
    Electronic Resource
    Electronic Resource
    Immobilized catalase-containing yeast cells: Preparation and enzymatic properties (1980)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 22 (1980), S. 2191-2205 
    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 cell of Saccharomyces cerevisiae previously induced for catalase (EC 1.11.1.6) activity were immobilized by entrapment of intact cells in acrylamide polymerized by γ irradiation (100 kR). Yeast cells showed an enhancement in catalase activity on entrapment, an effect similar to that observed on treatment with organic solvents like toluene. The cells pretreated with toluene, however, showed complete loss of catalase activity on entrapment. The entrapped enzyme exhibited a narrow pH optimum, reduced Km for H2O2, and a decrease in thermostability. The temperature optimum of catalase was also decreased from 60 to 40°C on immobilization. A tenfold decrease in the activation energy was also observed. The enzyme in the entrapped cells was, however, stable toward inactivation by γ irradiation. Unlike the intact cells, the entrapped yeast cells did not have the ability to induce catalase.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260221015
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  • 16
    Electronic Resource
    Electronic Resource
    Continuous conversion of sucrose to fructose and gluconic acid by immobilized yeast cell multienzyme complex (1980)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 22 (1980), S. 2179-2189 
    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 multienzyme complex consisting of invertase, glucose oxidase, and catalase was reconstituted by binding glucose oxidase using concanavalin A (Con A) to the cell wall of Sacchararomyces cerevisiae, previously induced for maximal activities of invertase and catalase. The cell flocculate obtained was stabilized by entrapment in polyacrylamide using γ irradiation at 100 kR. This complex showed a shortening of the lag period and enhancement in gluconic acid production as compared to a similar mixture of soluble enzymes. The efficacy of the multienzyme complex has been compared with that of mixed multienzyme system composed of individually immobilized enzymes. The immobilized multienzyme complex in a continuous-flow stirred-tank reactor system could be operated for continuous conversion of sucrose to fructose and gluconic acid. The reactor system did not show any loss in efficiency in a continuous operation over 20 days.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260221014
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  • 17
    Electronic Resource
    Electronic Resource
    Hen egg white: A novel support for the immobilization of enzymes (1981)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 23 (1981), S. 431-436 
    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: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260230217
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  • 18
    Electronic Resource
    Electronic Resource
    Hydrolysis of milk lactose by immobilized β-galactosidase-hen egg white powder (1984)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 26 (1984), S. 901-904 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Immobilized β-galactosidase was obtained by crosslinking the enzyme with hen egg white using 2% glutaraldehyde. The gel obtained could be lyophilized to give a dry enzyme powder. The pH optimum of both the soluble and immobilized enzyme was found to be 6.8. The immobilized enzyme showed a higher Km for the substrates. The extent of enzyme inhibition by galactose was reduced upon immobilization. The stability towards inactivation by heat, urea, gamma irradiation, and protease treatment were enhanced. The bound enzyme as tested in a batch reactor could be used repeatedly for the hydrolysis of milk lactose. The possible application of this system for small-scale domestic use has been suggested.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260260813
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  • 19
    Electronic Resource
    Electronic Resource
    Effect of modifying agents on immobilized alcohol dehydrogenase (1984)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 26 (1984), S. 544-545 
    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: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260260521
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  • 20
    Electronic Resource
    Electronic Resource
    The involvement of phenolics and phytoalexins in resistance of potato to soft rot (1984)
    Springer
    Potato research 27 (1984), S. 189-199 
    Details
    ISSN: 1871-4528
    Keywords: Erwinia carotovora var.carotovora ; disease resistance ; chlorogenic acid ; ferulic acid ; caffeic acid ; rishitin ; phytuberin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Summary Phenolics, for example chlorogenic, caffeic and ferulic acid, and phytoalexins, such as rishitin and phytuberin, were identified in potato tubers cv. Kufri Chandramukhi. The tissue of healthy tubers contained no detectable phytoalexins but did contain phenolics. The levels of these compounds were correlated with soft rot development. The rotting tissue either was free of these groups of compounds or had low concentrations. The wound periderm formed as a result of recovery from injury and infection contained high levels of the compounds. Much higher concentrations were detected at lower storage temperatures when oxygen supply was adequate. Antibacterial properties of the phenolics identified were tested againstErwinia carotovora which was inhibited by chlorogenic, caffeic and ferulic acids. The three phenolics were more effective together, in proportions in which they occurred in wound periderm, than individually. It was observed that none of these phenolics could inhibit pectolytic enzymes ofE. carotovora.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02357464
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