Catabolism of L-phenylalanine by some microorganisms of cheese origin

1984 ◽  
Vol 51 (3) ◽  
pp. 461-469 ◽  
Author(s):  
Chang-Won Lee ◽  
Jean Richard

SummaryThe ability of 42 microorganisms isolated from cheese, including strains of yeasts,Geotrichum candidum, Arthrobacter, Moraxellaspp.,Brevibacterium linensandStaphylococcus saprophyticusspp. to produce phenethyl alcohol (PEA) from L-phenylalanine was studied. All the yeast strains produced labelled PEA from L-[U-14C]phenylalanine. Phenylpyruvic acid was detected as an intermediate of PEA production and CO2was produced by decarboxylation of this acid. For five strains tested, the level of PEA which had accumulated in the culture at the end of exponential growth phase represented 39–52% of the L-Phe added. None ofG. candidumstrains nor bacterial isolates produced PEA from L-Phe. Strains ofMoraxellaspp. and four strains of theS. saprophyticusgroup produced phenylacetaldehyde. For three strains ofArthrobacterspp., five ofB. linensand all theMoraxella,14CO2produced from uniformly labelled L-Phe represented more than one carbon atom of the L-Phe molecule, suggesting that Phe was catabolized beyond the stage of phenylacetic acid. Production and disappearance of PEA during Camembert cheese ripening is probably related to the metabolic activity of microorganisms present at the cheese surface.

1998 ◽  
Vol 61 (10) ◽  
pp. 1281-1285 ◽  
Author(s):  
VIRGINIE DIEULEVEUX ◽  
MICHELINE GUÉGUEN

d-3-Phenyllactic acid is a compound with anti-Listeria activity which is produced and secreted by the yeastlike fungus, Geotrichum candidum. This compound has a bactericidal effect independent of the physiological State of Listeria monocytogenes when added at a concentration of 7 mg/ml to tryptic soy broth supplemented with yeast extract (TSB-YE). An initial L. monocytogenes population of 105 CFU/ml was reduced 100-fold (2 log) after 4 days of culture at 25 °C in TSB-YE containing d-3-phenyllactic acid. The Listeria population was reduced 1,000-fold (3 log) when the compound was added during the exponential growth phase, and was reduced to less than 10 CFU/ml when it was added during the stationary phase. d-3-Phenyllactic acid had a bacteriostatic effect in UHT whole milk, reducing the population by 4.5 log, to give fewer cells than in the control after 5 days of culture. The results obtained with L. monocytogenes at concentrations of 105 and 103 CFU/ml in cheese curds were less conclusive. d-3-Phenyllactic acid was 10 times less active than nisin in our experimental conditions (TSB-YE at 25°C).


2011 ◽  
Vol 38 (9) ◽  
pp. 11804-11812 ◽  
Author(s):  
M. Sicard ◽  
C. Baudrit ◽  
M.N. Leclerc-Perlat ◽  
P.H. Wuillemin ◽  
N. Perrot

1982 ◽  
Vol 49 (3) ◽  
pp. 501-510 ◽  
Author(s):  
Patrick Trieu-Cuot ◽  
Jean-Claude Gripon

SUMMABYIsoelectric focusing and 2-dimensional electrophoresis were used to study the development of the pH 4·6-insoluble fraction during Camembert cheese ripening. Modifications of this fraction were due mainly to the action of 5 proteinases: rennet (chymosin + bovine pepsin), plasmin and Penicillium caseicolum aspartyl-and metalloproteinases. Rennet was inactive on β-casein, but acted very early on αs1-casein. However, rennet and P. caseicolum aspartyl-proteinase had a very similar action on the latter substrate, which prevented clear definition of the respective actions of these proteinases on αs1-casein after 7 d of ripening. Plasmin action on β-casein was important from 21 and 35 d of ripening at the surface and in the centre of the cheese respectively, suggesting an important influence of pH changes during maturation. The respective activities of the metallo-and aspartyl-proteinases of P. caseicolum were characterized and followed using β-casein degradation products as markers. The metallo-proteinase activity was detectable immediately after the development of the Penicillium (7 d), while that of the aspartyl-proteinase was observed 3 d later. Thereafter, the amount of β-casein degradation peptides resulting from the metalloproteinase decreased while that resulting from the aspartyl-proteinase increased, suggesting a more important role of the latter enzyme.


1987 ◽  
Vol 58 (4) ◽  
pp. 356-358 ◽  
Author(s):  
Kei KATAOKA ◽  
Kazutaka NUKADA ◽  
Taku MIYAMOTO ◽  
Toshitaka NAKAE

Nematology ◽  
2008 ◽  
Vol 10 (1) ◽  
pp. 79-85 ◽  
Author(s):  
Li Cao ◽  
Xuehong Qiu ◽  
Xiaofen Liu ◽  
Xiuling Liu ◽  
Richou Han

Abstract Xenorhabdus and Photorhabdus bacteria are symbionts of entomopathogenic nematodes of the genera Steinernema and Heterorhabditis, respectively. To determine the nutrient potential of these bacteria for a free-living nematode, Panagrellus redivivus, a promising food source for first-feeding fish and crustacean, sterile first-stage juveniles (J1) of P. redivivus were fed on various isolates of Xenorhabdus and Photorhabdus bacteria in liquid cultures. Most of the tested bacterial isolates did not support the growth of P. redivivus. However, four of the Xenorhabdus isolates (X. nematophila All, X. bovienii T319, X. beddingii X-7 and X. poinarii KG) provided nutrients for the production of these nematodes in a liquid medium. Two Xenorhabdus isolates (X. beddingii X-7 and X. poinarii KG) even supported mass production of the nematode in a sponge medium, with yields comparable to those with yeast strains. This is the first report that Xenorhabdus bacteria can function as a nutrient source for mass production of nematodes other than their usual symbiotic partners.


2005 ◽  
Vol 15 (6-9) ◽  
pp. 883-891 ◽  
Author(s):  
K. Arfi ◽  
M.N. Leclercq-Perlat ◽  
H.E. Spinnler ◽  
P. Bonnarme

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