The Bacterial Reduction of Trimethylamine Oxide to Trimethylamine

1939 ◽  
Vol 4b (5) ◽  
pp. 367-377 ◽  
Author(s):  
H. L. A. Tarr

Only three of thirty microorganisms isolated from seven samples of fresh or lightly smoked sea fish muscle in various stages of decomposition reduced trimethylamine oxide to trimethylamine. This reduction is due to an enzyme, which activates trimethylamine oxide rendering it susceptible to reduction by many of the dehydrogenases of the bacterial cell. This enzyme, as it occurs in the intact cell, is apparently completely inhibited by toluene-treatment but not by cyanide. It. has not yet been obtained in cell-free state, and its substrate specificity has not been determined. Putrid fish muscle, with negligible amounts of trimethylamine, has been obtained by inoculating aseptically excised fish muscle with non-trimethylamine forming bacteria.

1939 ◽  
Vol 4b (4) ◽  
pp. 252-266 ◽  
Author(s):  
Dennis W. Watson

In fish muscle press juice simulating the surface and the interior of muscle, there is an aerobic environment in the surface layer and an anaerobic environment in the body of the liquid. The Eh potential of the former is about 0.3 volts and of the latter from −0.5 to −0.10 volt.It is found that the bacterial population proliferating at 2 °C. is chiefly Achromobacter, which can be divided into two groups, obligate aerobes and facultative anaerobes. Only the latter group, which is capable of growth in the interior or surface, is responsible for the reduction of trimethylamine oxide with the evolution of trimethylamine. Since the initial total count is made up of a large number of obligate aerobes or non-oxide reducers it is obvious that the total bacterial population cannot be related to trimethylamine production. The appearance of this base therefore may be taken to indicate a bacterial population which is in excess of that responsible for its production.Molecular oxygen at surface exercises a trimethylamine oxide sparing effect. In practice, however, this effect is not significant from the point of view of the freshness test in the sense of Beatty and Gibbons.


1958 ◽  
Vol 24 (8) ◽  
pp. 645-647 ◽  
Author(s):  
Yoshiro HASHIMOTO ◽  
Tomotoshi OKAICHI

Microbiology ◽  
1985 ◽  
Vol 131 (6) ◽  
pp. 1357-1361
Author(s):  
J. D. OWENS ◽  
D. R. MISKIN ◽  
M. C. WACHER-VIVEROS ◽  
L. C. A. BENGE

1950 ◽  
Vol 7d (10) ◽  
pp. 567-575 ◽  
Author(s):  
C. H. Castell

In the presence of bacteria capable of reducing it, trimethylamine oxide exerts a poising action on the oxidation-reduction potentials of media. This poising is at an Eh level considerably electropositive to the Eó of the redox indicators commonly used in the "reduction tests" used for determining the bacterial quality of foods.


1949 ◽  
Vol 7c (8) ◽  
pp. 461-470 ◽  
Author(s):  
W. J. Dyer

Bacteria reduce sodium nitrite in stored cod fillets. Rapid reduction of trimethylamine oxide is inhibited by the nitrite in the concentrations used, up to 700 p.p.m., trimethylamine formation occurring only after the nitrite is reduced to about 50 p.p.m. This results in an increased keeping time in fillets treated with nitrite. The surface pH remains acid until the rapid trimethylamine formation takes place.Nitrate alone, more slowly in the presence of nitrite, is rapidly reduced to nitrite and beyond. The trimethylamine oxide reduction is not affected by the nitrate reduction, the former being usually reduced before the nitrate.


2018 ◽  
Author(s):  
Richard Nemeth ◽  
Mackenzie Neubert ◽  
Thomas Ni ◽  
Christopher J. Ackerson

In the present work we have identified a glutathione reductase like metalloid reductase (GRLMR) responsible for mediating selenite tolerance in <i>Pseudomonas moravenis</i> stanleyae through the enzymatic generation of Se(0) nanoparticles. This enzyme has an unprecedented substrate specificity for selenodiglutathione (K<sub>m</sub>= 336 μM) over oxidized glutathione (K<sub>m</sub>=8.22 mM). This enzyme was able to induce selenite tolerance in foreign bacterial cell lines by increasing the IC<sub>90</sub> for selenite from 1.9 mM in cell lacking the GRLMR gene to 21.3 mM for cells containing the GRLMR gene. It was later confirmed by STEM and EDS that Se nanoparticles were absent in control cells and present in cells expressing GRLMR. Structural analysis suggests the lack of a sulfur residue in the substrate/product binding pocket may be responsible for this unique substrate specificity.


2003 ◽  
Vol 185 (7) ◽  
pp. 2259-2266 ◽  
Author(s):  
Petra J. Edqvist ◽  
Jan Olsson ◽  
Moa Lavander ◽  
Lena Sundberg ◽  
Åke Forsberg ◽  
...  

ABSTRACT Pathogenic Yersinia species use a type III secretion system to inhibit phagocytosis by eukaryotic cells. At 37°C, the secretion system is assembled, forming a needle-like structure on the bacterial cell surface. Upon eukaryotic cell contact, six effector proteins, called Yops, are translocated into the eukaryotic cell cytosol. Here, we show that a yscP mutant exports an increased amount of the needle component YscF to the bacterial cell surface but is unable to efficiently secrete effector Yops. Mutations in the cytoplasmic domain of the inner membrane protein YscU suppress the yscP phenotype by reducing the level of YscF secretion and increasing the level of Yop secretion. These results suggest that YscP and YscU coordinately regulate the substrate specificity of the Yersinia type III secretion system. Furthermore, we show that YscP and YscU act upstream of the cell contact sensor YopN as well as the inner gatekeeper LcrG in the pathway of substrate export regulation. These results further strengthen the strong evolutionary link between flagellar biosynthesis and type III synthesis.


1952 ◽  
Vol 8c (5) ◽  
pp. 314-324 ◽  
Author(s):  
W. J. Dyer

Original determinations of the trimethylamine oxide content of 60 species of fish are recorded, and 21 additional species have been studied by others. Elasmobranchs have the highest content of oxide, two to five per cent based on dry weight. Among teleost fishes, the amount increases from the lower to the higher orders, freshwater fish containing no oxide. Analyses of several species of marine invertebrates confirm earlier work showing that certain molluscs, echinoderms and other organisms contain trimethylamine oxide, often in quantities similar to those in the higher teleosts.


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