Occurrence of arginine deiminase pathway enzymes in arginine catabolism by wine lactic Acid bacteria

Abstract

L-Arginine, an amino acid found in significant quantities in grape juice and wine, is known to be catabolized by some wine lactic acid bacteria. The correlation between the occurrence of arginine deiminase pathway enzymes and the ability to catabolize arginine was examined in this study. The activities of the three arginine deiminase pathway enzymes, arginine deiminase, ornithine transcarbamylase, and carbamate kinase, were measured in cell extracts of 35 strains of wine lactic acid bacteria. These enzymes were present in all heterofermentative lactobacilli and most leuconostocs but were absent in all the homofermentative lactobacilli and pediococci examined. There was a good correlation among arginine degradation, formation of ammonia and citrulline, and the occurrence of arginine deiminase pathway enzymes. Urea was not detected during arginine degradation, suggesting that the catabolism of arginine did not proceed via the arginase-catalyzed reaction, as has been suggested 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 containing relatively high concentrations (>0.5%) of fructose, ammonia formation is inhibited.

Amino acid transport in Lactobacillus helveticus

“…These enzymes could not be detected in L. helveticus (data not shown). Recently, Liu et al [14] reported the presence of arginine deimidase in hetero-fermentative but not in homo-fermentative lactobacilli. Our results are consistent with this conclusion.…”

Evolution of amino acids and biogenic amines in natural ciders as a function of the year and the manufacture steps

“…Another relevant finding was the reduction or disappearance of arginine during the manufacture of the ciders studied, which could be explained in function of the complex microbiological interactions along natural cider production, as alcoholic and MLF occur simultaneously, and microbiological stabilization is not performed. Thus, high levels of heterofermentative LAB found after MLF (Duen˜as et al, 1994) might degrade this amino acid via the arginine deiminase pathway, producing citrulline and carbamyl phosphate (Liu et al, 1995). In addition, it has also been described that some yeast could also degrade this amino acid producing urea and other carbamylic compounds as intermediates of arginine metabolism.…”

Acetaldehyde metabolism by wine lactic acid bacteria

“…Resting cell experiments were performed according to Mira de Ordun ¬ a et al [16] with modi¢cations. Bacterial cells were grown in 500 ml of a complex medium (TJAG [17], without addition of arginine) at 30³C to the late-exponential phase and harvested by centrifugation at 5000Ug for 10 min at 15³C. Yeast cells were grown in 500 ml YM broth (Difco, Detroit, MI, USA).…”