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  • 1
    Electronic Resource
    Electronic Resource
    Einfluß des Erhitzens auf Löslichkeit und Elektrophoreseverhalten der Sarkoplasmaproteine von Rind- und Schweinefleisch (1990)
    Springer
    European food research and technology 190 (1990), S. 223-227 
    Details
    ISSN: 1438-2385
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Description / Table of Contents: Zusammenfassung Die Hitzestabilität der Sarkoplasmaproteine bei Rind- und Schweinefleisch wurde anhand der Löslichkeit und der Proteinmuster nach elektrophoretischer Auftrennung untersucht. Als Untersuchungsmethoden kamen die Proteinbestimmung nach Bradford und die isoelektrische Focussierung in rehydratierbaren Polyacrylamidgelen zur Anwendung. Die focussierten Proteine wurden mit Hilfe der Silberfärbung sichtbar gemacht. Die Gesamtproteinkonzentrationen der Extrakte verringerten sich bis zu einer Temperatur von 80°C mit zunehmender Höhe und Dauer der Hitzebelastung. Bei den auf 100°C erhitzten Proben nahmen die Proteinkonzentrationen wieder geringfügig zu. Die Intensität der Proteinbanden nahm allgemein mit steigender Temperatur und Erhitzungszeit ab. Die deutlichsten Änderungen der Bandenmuster zeigten sich im untersuchten Temperaturbereich bei dem auf 100°C erhitzten Fleisch. Durch eine Nacherhitzung der Fleischproben konnten erhitzungsbedingte Unterschiede in den Bandenmuster ausgeglichen werden. Auf diese Weise ist eine elektrophoretische Tierartenidentifizierung bei erhitztem Fleisch unabhängig von der Kenntnis der Erhitzungsbedingungen möglich.
    Notes: Summary The heat stability of sarcoplasmic proteins of beef and pork was investigated by means of their solubility and their protein patterns after electrophoretic separation. The method of determination of proteins described by Bradford and isoelectric focusing in rehydratable polyacrylamide gels were used for these investigations. The electrofocused proteins were visualized by silver staining. The concentration of total protein of the extracts decreased with increase in temperature and heating time (up to a temperature of 80° C). However the protein concentration increased in samples heated to 100° C. The intensity of the protein bands decreased with increasing temperature and heating time. In the investigated range of temperature, variations in protein patterns were most significant in meat heated to 100° C. Differences of protein pattern caused by different heating conditions could be equalized by a second heating of the samples. In this way it is possible to identify meat species without knowing the heating conditions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01192970
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  • 2
    Electronic Resource
    Electronic Resource
    Einfluß des Erhitzens auf die Löslichkeit und das Elektrophoreseverhalten von Myoglobin (1990)
    Springer
    European food research and technology 190 (1990), S. 414-419 
    Details
    ISSN: 1438-2385
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Description / Table of Contents: Zusammenfassung Die Hitzestabilität des Myoglobins bei Rindfleisch wurde anhand seiner Löslichkeit und der Intensität der Proteinmuster nach isoelektrischer Focusierung untersucht. Für die empfindliche Bestimmung von Myoglobin in den Extrakten wurde eine photometrische Methode entwickelt, die auf einer durch Myoglobin katalysierten oxidativen Kupplung von 2,4-Dichlorphenol und 4-Aminoantipyrin in Gegenwart von Wasserstoffperoxid beruht, wobei ein roter Farbstoff gebildet wird. Mit dieser Methode konnten noch Myoglobinkonzentrationen bis 0,01 mg/ml erfaßt werden. Für den Nachweis der elektrofocussierten Myoglobine erwies sicho-Dianisidin von den untersuchten Substraten als am empfindlichsten. Die Myoglobingehalte der Extrakte nahmen mit steigender Hitzebelastung des Fleisches ab. Dementsprechend sank auch die Intensität der Myoglobinbanden mit steigender Temperatur und zunehmender Dauer der Erhitzung, ihre Lage im Elektrophoresegel blieb jedoch unverändert.
    Notes: Summary The heat stability of beef myoglobin was investigated by means of its solubility and intensity of protein bands separated by isoelectric focusing. A method for the sensitive determination of myoglobin in the extracts was developed based on its ability to form a red dye by the oxidative coupling of 2,4-dichlorophenol and 4-aminoantipyrine in the presence of hydrogen peroxide. By this method, myoglobin could be determined to a concentration of 0.01 mg/ml. For the detection of electro-focused myoglobins,o-dianisidine has proved to be the most sensitive compound. The myoglobin content of the extracts, according to the intensity of the myoglobin bands in the electrophoretic gel, decreased with increasing temperature and heating-time. However, the position of the bands was not changed by the heat treatment.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01202559
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  • 3
    Electronic Resource
    Electronic Resource
    Degradation and dehalogenation of monochlorophenols by the phenol-assimilating yeast Candida maltosa (1991)
    Springer
    Biodegradation 2 (1991), S. 193-199 
    Details
    ISSN: 1572-9729
    Keywords: Candida maltosa ; monochlorophenols ; chlorocatechol ; chloromuconic acid ; dechlorination mechanism ; phenol hydroxylase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Energy, Environment Protection, Nuclear Power Engineering , Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract The phenol-assimilating yeast Candida maltosa is able to degrade monochlorophenols but cannot grow on these substrates. 3- and 4-chlorophenol were broken down very rapidly by phenol-grown cells under the formation of 4-chlorocatechol, 5-chloropyrogallol and 4-carboxymethylenebut-2-en-4-olide with concomitant release of chloride. 2-Chlorophenol was partially converted into cis,cis-2-chloromuconic acid via 3-chlorocatechol which was also obtained from 3-chlorophenol in low amounts. No further metabolites containing chloride were found. The dehalogenation step in the chlorophenol degradation is the cycloisomerization of the cis,cis-chloromuconic acid to 4-carboxymethylenebut-2-en-4-olide in the ortho fission pathway.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00124493
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  • 4
    Electronic Resource
    Electronic Resource
    An expression vector system providing plasmid stability and conditional suicide of plasmid-containing cells (1992)
    Springer
    Applied microbiology and biotechnology 38 (1992), S. 91-93 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary A cloning vector system was constructed on the basis of the pBR322 derivative pEG1 by introducing the whole parB locus of plasmid R1 cloned behind the promoter of the alkaline phosphatase gene (phoA) of Escherichia coli. The parB locus in combination with the phoA promoter ensures both (i) plasmid stabilization due to the post-segregational killing of plasmid-free cells during growth and (ii) killing of the cells induced by the potential environmental signal phosphate limitation. This vector, therefore, appears to be a model system for increasing the stability of recombinant plasmids and for decreasing the potential risks in the application of recombinant bacteria in industrial fermentations.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00169425
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  • 5
    Electronic Resource
    Electronic Resource
    Catabolite inactivation, cyclic AMP and protein phosphorylation in the methylotrophic yeastHansenula polymorpha (1991)
    Springer
    Antonie van Leeuwenhoek 60 (1991), S. 49-54 
    Details
    ISSN: 1572-9699
    Keywords: alcohol oxidase ; catabolite inactivation ; cyclic AMP ; Hansenula polymorpha ; protein phosphorylation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The inactivation of the peroxisomal enzyme alcohol oxidase and the cytoplasmic enzymes fructose-1,6-bisphosphatase, malate dehydrogenase and phosphoenolpyruvate carboxykinase was found to occur after addition of glucose to methanol-grown cells of the yeastHansenula polymorpha. The concentration of cyclic AMP increased nearly twofold within 3 min under the same conditions. In crude extracts ofH. polymorpha about 20 proteins are phosphorylated by cyclic AMP dependent protein kinases, among them also fructose-1,6-bisphosphatase. No phosphorylation of the alcohol oxidase protein could be detected. From this fact, it was concluded that the inactivation of the peroxisomal alcohol oxidase is independent of cyclic AMP-dependent protein phosphorylation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00580441
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