INVESTIGADORES
FADDA silvina graciela
artículos
Título:
Preliminary characterization of Ò-decarboxylase activities in Staphylococcus carnosus 833, a strain used in sausage fermentation
Autor/es:
FADDA, S.; LEROY, S.; TALON, R.
Revista:
FEMS MICROBIOLOGY LETTERS
Editorial:
FEMS
Referencias:
Lugar: Reading (UK); Año: 2003 p. 143 - 149
ISSN:
0378-1097
Resumen:
In sausage, Staphylococcus carnosus increases the levels of methyl ketones which could arise from incomplete L-oxidation of fatty acids
followed by a decarboxylation. The objective of this work was to characterize the L-decarboxylase activities in cell-free extract. By using
different substrates, at least two kinds of L-decarboxylase activities were shown: an acetoacetate-like and an oxaloacetate-like. The first
one leads to the production of ketones from ethylbutyryl acetate or acetoacetic acid. The activity was optimal at pH 6.0, stimulated by
pyridoxal phosphate but ethylenediamine tetraacetic acid (EDTA), NaCl, iodoacetate and curing additives were inhibitory. The second
decarboxylase activity leads to the production of pyruvic acid from oxaloacetic acid. This activity was optimal at pH 5.0 and stimulated
by divalent ions and biotin.Staphylococcus carnosus increases the levels of methyl ketones which could arise from incomplete L-oxidation of fatty acids
followed by a decarboxylation. The objective of this work was to characterize the L-decarboxylase activities in cell-free extract. By using
different substrates, at least two kinds of L-decarboxylase activities were shown: an acetoacetate-like and an oxaloacetate-like. The first
one leads to the production of ketones from ethylbutyryl acetate or acetoacetic acid. The activity was optimal at pH 6.0, stimulated by
pyridoxal phosphate but ethylenediamine tetraacetic acid (EDTA), NaCl, iodoacetate and curing additives were inhibitory. The second
decarboxylase activity leads to the production of pyruvic acid from oxaloacetic acid. This activity was optimal at pH 5.0 and stimulated
by divalent ions and biotin.L-decarboxylase activities in cell-free extract. By using
different substrates, at least two kinds of L-decarboxylase activities were shown: an acetoacetate-like and an oxaloacetate-like. The first
one leads to the production of ketones from ethylbutyryl acetate or acetoacetic acid. The activity was optimal at pH 6.0, stimulated by
pyridoxal phosphate but ethylenediamine tetraacetic acid (EDTA), NaCl, iodoacetate and curing additives were inhibitory. The second
decarboxylase activity leads to the production of pyruvic acid from oxaloacetic acid. This activity was optimal at pH 5.0 and stimulated
by divalent ions and biotin.L-decarboxylase activities were shown: an acetoacetate-like and an oxaloacetate-like. The first
one leads to the production of ketones from ethylbutyryl acetate or acetoacetic acid. The activity was optimal at pH 6.0, stimulated by
pyridoxal phosphate but ethylenediamine tetraacetic acid (EDTA), NaCl, iodoacetate and curing additives were inhibitory. The second
decarboxylase activity leads to the production of pyruvic acid from oxaloacetic acid. This activity was optimal at pH 5.0 and stimulated
by divalent ions and biotin.