Sq. Liu et al., OCCURRENCE OF ARGININE DEIMINASE PATHWAY ENZYMES IN ARGININE CATABOLISM BY WINE LACTIC-ACID BACTERIA, Applied and environmental microbiology, 61(1), 1995, pp. 310-316
L-Arginine, an amino acid found in significant quantities in grape jui
ce and wine, is known to be catabolized by some wine lactic acid bacte
ria. The correlation between the occurrence of arginine deiminase path
way enzymes and the ability to catabolize arginine was examined in thi
s study. The activities of the three arginine deiminase pathway enzyme
s, arginine deiminase, ornithine transcarbamylase, and carbamate kinas
e, were measured in cell extracts of 35 strains of wine lactic acid ba
cteria. These enzymes were present in all heterofermentative lactobaci
lli and most leuconostocs but were absent in all the homofermentative
lactobacilli and pediococci examined. There was a good correlation amo
ng arginine degradation, formation of ammonia and citrulline, and the
occurrence of arginine deiminase pathway enzymes. Urea was not detecte
d during arginine degradation, suggesting that the catabolism of argin
ine did not proceed via the arginase-catalyzed reaction, as has been s
uggested in some earlier studies. Detection of ammonia with Nessler's
reagent was shown to be a simple, rapid test to assess the ability of
wine lactic acid bacteria to degrade arginine, although in media conta
ining relatively high concentrations (>0.5%) of fructose, ammonia form
ation is inhibited.