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  • 1
    Electronic Resource
    Electronic Resource
    A population balance model of enzymatic lysis of microbial cells (1990)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 35 (1990), S. 31-42 
    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 model is proposed for enzymatic lysis of microbial cells based on number balances over the distribution of cell-wall mass in a population of cells. Analytical solutions to the population balance equations were obtained by the method of characteristics for simple reaction kinetics. The model has been used to analyze the following cases of lysis in a nonhomogeneous cell population: wall hydrolysis with cell rupture and product release, the effect of a distribution of lysis rates, and lysis of two-layer cell walls. Rate expressions for the reactions of lysis can be derived from bulk-phase experiments; the distributions of cell size and product content can be measured independently by flow cytometric techniques. The population model also provides an explanation for the initial lag seen in lysis kinetics for virtually any initial distribution. The model demonstrates patterns of lysis and product recovery for heterogeneous populations of cells and also applies to the more general problem of soluble-enzyme reactions with heterogeneous solid substrates.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260350106
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  • 2
    Electronic Resource
    Electronic Resource
    Kinetics of enzymatic lysis and disruption of yeast cells: I. Evaluation of two lytic systems with different properties (1987)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 30 (1987), S. 471-480 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Many microorganisms produce enzymes which lyse the walls of yeasts, fungi, and bacteria. The proportions of different enzyme activities present in the lytic system, their action patterns, synergism, and dependence on inhibitors, constitute the activity profile of the lytic system. Taken together, the activity profile and process conditions for lysis determine the reaction rate and the distribution of products from lysis of any given type of cells. Kinetics of glucan hydrolysis, proteolysis, and lysis of brewer's yeast were compared for two extracellular yeast-lytic enzyme systems with different properties. The enzyme sources used were filtered culture broths from Cytophaga sp. NCIB 9497 grown in batch culture and from Oerskovia xanthineolytica LL-G109, grown under carbon limitation in continuous culture. Rate and extent of cell hydrolysis, and the accumulation of soluble proteins, peptides, and carbohydrates from the lysed yeast cells, are discussed in terms of the activity profiles and potential applications of the two enzyme systems.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260300403
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  • 3
    Electronic Resource
    Electronic Resource
    A structured mechanistic model of the kinetics of enzymatic lysis and disruption of yeast cells (1988)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 31 (1988), S. 929-943 
    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 structured, mechanistic model has been built for the kinetics of yeast cell lysis by microbial cell lytic enzymes, based on an understanding of the two-layer yeast cell wall structure and the properties of yeast-lytic enzyme systems. The model predicts the release of protein, peptides and carbohydrates from four cell structures: the outer and inner wall layers, the cytosol and organelles or proteins present in particles; it also predicts organelle or particle lysis or solubilization and the breakdown of released proteins to peptides. Applications of the model to design and optimization of selective product release are discussed.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260310906
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  • 4
    Electronic Resource
    Electronic Resource
    Kinetics of enzymatic lysis and disruption of yeast cells: II. A simple model of lysis kinetics (1987)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 30 (1987), S. 481-490 
    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 simple two-step model is proposed to describe the kinetics of the two lytic systems examined in the preceding article. The model predicts concentrations of yeast solids, soluble proteins, peptides, and carbohyrates. In the first reaction step, yeast cell mass is solubilized; in the second, the released protein can be hydrolyzed to peptides. Kinetics for both yeast lysis and the subsequent protein breakdown are based on Michaelis-Menten expressions. Terms have been included for competitive inhibition of yeast lysis by substances in the Cytophaga enzyme preparation, and for incomplete hydrolysis of cells by the Oerskovia enzyme system. Parameters have been independently determined for all reactions except Oerskovia proteolysis, where they were fit by a leastsquares method to data from model test runs. The model has been verified for yeast concentrations between 0.7 and 70 g/L yeast (dry basis) and 4-40% crude enzyme solution.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260300404
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