FERMENTATION OF ALPHA KETO ACIDS BY MICROCOCCUS AEROGENES AND MICROCOCCUS LACTILYTICUS
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چکیده
منابع مشابه
Fermentation of amino acids by Micrococcus aerogenes.
The anaerobic micrococci described by Foubert and Douglas (1948a) may be divided into 3 groups on the basis of ability to degrade organic compounds: (1) those capable of fermenting only glycine (Douglas, 1951), (2) those able to degrade purines (Whiteley and Douglas, 1951) and many organic acids (Foubert and Douglas, 1948b), and (3) those able to ferment purines and a limited number of amino ac...
متن کاملDegradation of Pyruvate by Micrococcus Lactilyticus
MICCORnMICK, N. G. (University of W1'ashington, Seattle), E. J. ORDAL, AND H. R. WHITELEY. Degradation of p)yruvate by Micrococcus lactilyticus. II. Studies of cofactors in the formate-exchange reaction. J. Bacteriol. 83:899-906. 1962. Enzyme preparations from ilicrococcus lactilyticus2 are rendered inactive with respect to formate exchange by treatment with charcoal or Dowex-5O, by dialysis, o...
متن کامل2%Oxypurine Dehydrogenase from Micrococcus aerogenes
Extracts of Micrococcus aerogenes, an anaerobe capable of fermenting purines, contain two enzymes which catalyze the oxidation of 2-oxypurine. These have been purified and separated from one another. One has the broad substrate specificity typical of xanthine dehydrogenase; the other is very specific with regard to the substrates oxidized and will only oxidize 2-oxypurine and closely related co...
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This study presents biodegradation of benzoic acid (BA) and anthranilic acid (AA) by Micrococcus sp. under aerobic conditions. Initial concentrations of BA and AA were varied (500-2500 mg/l) and almost complete biodegradation of BA and AA was observed within 30 h. Andrews kinetic model for single substrate was fitted to obtain maximum specific growth rates, half saturation and substrate inhibit...
متن کاملThe isolation and characterization of malate-lactate transhydrogenase from Micrococcus lactilyticus.
The malate-lactate transhydrogenase of Micrococcus lactilyticus has been purified and found to be a colorless protein with a molecular weight of approximately 99,000. The enzyme catalyzes the transfer of hydrogen from 3and 4carbon straight chain L-cu-hydroxy acids to cY-keto acids. The reactions catalyzed are readily reversible and the K,, (L-malate) (pyruvate)/(oxalacetate) (L-lactate) = 1.8. ...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1957
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.74.3.331-336.1957