Growth Characteristics of Pseudomonas fluorescens on Ovalbumin Substrates
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چکیده
منابع مشابه
Effect of carbon dioxide on growth of Pseudomonas fluorescens.
In minimal medium at 30 degrees C, growth of Pseudomonas fluorescens was stimulated when the pressure (p) of CO2 in solution was 100 mm of Hg, but at higher concentrations the growth rate declined linearly with increasing pCO2. All concentrations of CO2 were inhibitory for growth in complex medium, and at 30 degrees C the maximum degree of inhibition was attained when pCO2 was 250 mm of Hg. The...
متن کاملPseudomonas fluorescens
nas incognita have been previously described as being able to utilize citronellol, geraniol, and linalool (3, 6). Recently, a 50-megadalton (MDa) plasmid has been associated with the degradation of geraniol (9). In this report we describe the isolation of a Pseudomonas fluorescens s train capable of utilizing linalool as a sole carbon and energy source and demonstrate the presence of a transmis...
متن کاملSome characteristics of proteolytic enzymes from Pseudomonas fluorescens.
Our interest was stimulated by observing the active proteolytic abilities of a culture of Pseudomonas fluorescens isolated from a frozen chicken pie. The culture liquified gelatin rapidly and attacked casein strongly. In addition, the culture displayed considerable lipolytic and amylolytic activity. The culture was isolated from a tryptone-glucose-meat-extract-agar plate after incubation at 5 C...
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Aspartate transcarbamylase from a Pseudomonas fluerescens has been purified to homogeneity. The enzyme has a molecular weight of 360,000. It is composed of 2 apparently identical subunits with molecular weights of 180,000. Activity can be recovered from the enzyme denatured with mercaptoethanol and sodium dodecyl sulfate when the dodecyl sulfate is dialyzed away. The renatured enzyme has the mo...
متن کاملThe kynureninase of Pseudomonas fluorescens.
Kotake and Nakayama (1) observed the conversion of kynurenine to anthranilic acid and alanine by a mammalian liver extract. Subsequently the enzyme responsible for this reaction in the mammal was partly purified (2,3) and the enzyme, prepared from vitamin Be-deficient animals, was shown to require pyridoxal phosphate for its maximal activity (2). During an investigation of tryptophan metabolism...
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ژورنال
عنوان ژورنال: Poultry Science
سال: 1968
ISSN: 0032-5791
DOI: 10.3382/ps.0471780