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  • Biochemistry and Biotechnology  (5)
  • pH  (1)
  • poly-β-hydroxybutyrate  (1)
  • 1
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 30 (1987), S. 628-637 
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: This article describes the synthesis and regulation of β(1-3)glucanase and protease enzymes from the cell lytic system of Oerskovia xanthineolytica LL-G109 in continuous culture using different concentrations of carbon source (glucose) and inducer (glucan). These two enzyme activities are the main components of a lytic system capable of lysing and disrupting whole yeast cells; it is subject to catabolite repression by glucose and is induced by yeast glucan. Peaks of β(1-3)glucanase and protease activity are obtained at dilution rates of between 0.05 and 0.15 h-1. The glucanase-protease ratio is very high compared to other strains. At dilution rates above 0.15 h-1 all activities are similar to those obtained in batch culture. The lytic enzyme system appears to contain several β(1-3)glucanase enzymes. In continuous culture both productivity and enzyme concentrations are greatly in creased when compared to batch culture, 11- and 4.4-fold, respectively.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 38 (1991), S. 977-985 
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A novel method has been developed for the separation of bioproducts from yeast cells. The method uses a combination of physical, chemical, and biological agents such as lytic enzymes, osmotic supports, and spheroplast stabilizers. Using this technique, products (proteins and enzymes) can be released from specific cell locations at different process states; it has thus been celled differential product release (DPR). The wall-associated proteins are released first and the lytic enzyme is removed together with the wall proteins at this stage. Secondly, the cytosol products are released by a mild procedure during which the organelles remained intact. Finally, the organelle proteins are solubilized. In each stage, specific proteins are released while others are kept inside the different cell compartments. This method can be used with relatively high yeast concentrations (up to 145 g dry wt/L) and gives higher product recoveries and much higher selectivity than mechanical disruption.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 28 (1986), S. 1366-1375 
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Lytic enzyme systems with the ability to break whole cells of yeast are a mixture of several enzymes and virtually all contain β(1-3)glucanases and some protease. It appears that the presence of these two enzyme activities is necessary to break the two layers of the rigid cell wall. The enzyme system of Cytophaga NCIB 9497 has a high activity towards the walls of yeast and also of bacteria. This article describes the production of this extracellular lytic enzyme system in batch and continuous culture - it was found to be inducible. The synthesis and regulation of the two main constituent enzymes, β(1-3)glucanase and protease, have been investigated. The synthesis of β(1-3)glucanase is regulated by bothinduction (by an unknown inducer) and catabolite repression. Highβ(1-3)glucanase activities were obtained in continuous culture at low dilution rates over a narrow range (0.05-0.10 h-1), and there is evidence of the presence of more than one glucanase enzyme. Proteolytic activity appears subject to catabolite repression and made up of the activities of more than one protease enzyme. Productivity and enzyme concentration were increased several fold in continuous culture when compared to batch culture.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 43 (1994), S. 1052-1058 
    ISSN: 0006-3592
    Keywords: reversed micelle systems ; partition of proteins ; pH ; ionic strength ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Four proteins with different physicochemical properties have been partitioned in reversed micelle systems: thaumatin, ribonuclease A, soybean trypsin inhibitor, and α-lactalbumin. The organic phase was formed by sodium salt (AOT) in isooctane, and the aqueous phase contained KCl, KBr, MgCl2, or NaCl. Aqueous phase pH was varied between 2 and 13 and ionic strength from 0.1 to 1.0 M. Small changes in pH [around the isoelecric point (pl)] were found to influence the solubilization of ribonuclease A and trypsin inhibitor, but for thaumatin the pH change necessary to affect partition was much greater as a consequence of the difference in net charge (titration curves) of these protein molecules as pH changes. The type of ions present in the system was also a determining factor for partition; the larger ions (K+) produced more electrostatic screening and hence less protein solubilization than the smaller ions (Na+). With changes in ionic strength surface hydrophobicity was a dominant factor affecting solubilization of thaumatin in NaCl-containing systems at high pH. Charge distribution and hydrophobicity are thought to be important parameters when partitioning the protein α-lactalbumin. © 1994 John Wiley & Sons, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 46 (1995), S. 497-502 
    ISSN: 0006-3592
    Keywords: poly-β-hydroxybutyrate ; molcular weight distribution ; Alcaligens eutrophus ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The effect of magnesium and phosphate limitation on the molecular weight distribution of poly-β-hydroxybutyrate (PHB) in Alcaligens europhus in cotinuons culture has been stuied. Conditions of nitrogen limitation both with glucose excess (above ca. 20 g/L) and without excess were investigated Under N-limitation and glucose excess, Mw decreases when the magnesium content is decreased below 50% (19.7 mg/L) of the basal medium content; this also results in a broadenng of molecular weight distribution (Mw/Mn) from 2 to 5 and a decrease in Mw fron 2 × 106 to 0.9 × 106. Below 20% of the basal content of magnesium (7.9 mg/L) these two trends were reversed. This behaviour was not observed in the absence of glucose excess, phshate had virtually no effect on PHB Mw or its distribution, whereas wih no (or little) glucose excess Mw of the PHB decreased with phosphate concentrations below 50% of the basal level (0.705 g/L). Hence, in continuous or fed-batch cultures, in addition to nitrogen limitation to alklow for PHB accumulation, it is necesary to control both the addition of glucose (no excess) and also to maintain magnesium limitation (ca. 25% of basal medium level, 9.9 mg/L) and phosphate above 50% of he basal level (0.705 g/L). Thus, when broadening of molecular weight destribution (increase in Mw/Mn) is observed at the end of fed-batch culture it is probably caused by phosphate limitation and/or glucose excess. © 1995 John Wiley & Sons, Inc.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
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