(Table 1) Os and Sr isotopes in low-temperature hydrothermal fluids from the Juan de Fuca Ridge at ODP Site 168-1026B

We present Os and Sr isotopes and Mg, Os, and Sr concentrations for ridge-crest high-temperature and diffuse hydrothermal fluids, plume fluids and ridge-flank warm spring fluids from the Juan de Fuca Ridge. The data are used to evaluate the extent to which (1) the high- and low-temperature hydrothermal alteration of mid-ocean ridge basalts (MORBs) provides Os to the deep oceans, and (2) hydrothermal contributions of non-radiogenic Os and Sr to the oceans are coupled. The Os and Sr isotopic ratios of the high-temperature fluids (265-353°C) are dominated by basalts (187Os/188Os = 0.2; 87Sr/86Sr = 0.704) but the concentrations of these elements are buffered approximately at their seawater values. The 187Os/188Os of the hydrothermal plume fluids collected ~1 m above the orifice of Hulk vent is close to the seawater value (=1.05). The low-temperature diffuse fluids (10-40°C) associated with ridge-crest high-temperature hydrothermal systems on average have [Os] = 31 fmol/kg, 187Os/188Os = 0.9 and [Sr] = 86 µmol/kg, 87Sr/86Sr = 0.709. They appear to result from mixing of a high-temperature fluid and a seawater component. The ridge-flank warm spring fluids (10-62°C) on average yield [Os] = 22 fmol/kg, 187Os/188Os = 0.8 and [Sr] = 115 µmol/kg, 87Sr/86Sr = 0.708. The data are consistent with isotopic exchange of Os and Sr between basalt and circulating seawater during low-temperature hydrothermal alteration. The average Sr concentration in these fluids appears to be similar to seawater and consistent with previous studies. In comparison, the average Os concentration is less than seawater by more than a factor of two. If these data are representative they indicate that low-temperature alteration of MORB does not provide adequate non-radiogenic Os and that another source of mantle Os to the oceans must be investigated. At present, the magnitude of non-radiogenic Sr contribution via low-temperature seawater alteration is not well constrained. If non-radiogenic Sr to the oceans is predominantly from the alteration of MORB, our data suggest that there must be a different source of non-radiogenic Os and that the Os and Sr isotope systems in the oceans are decoupled.

Identifying yeats belonging to the Brettanomyces/Dekkera genera through the use of selective-differential media

The purpose of this work was to compare and optimise different selective and differential media to aid in isolating spoilage yeasts belonging to the Brettanomyces/Dekkera genera. Growth media containing selective and differential factors were employed. These were inoculated with strains of yeast representing Spanish oenological microbiota. Lastly, some of these isolation media were successfully applied in 24 types of wine with a high ethylphenol content, all of which were from the Haro Oenological Station (La Rioja, Spain). p-coumaric acid was determined using High performance liquid chromatography-photodiode-array detection-electrospray ionization mass spectrometry (HPLC-DAD-ESI/MS); 4-ethylphenol by using Solid phase micro extraction-gas chromatography-mass spectrometry (SPME-GC-MS); and the rest of the analysis was carried out using official OIV methodology. Actidione is the most effective selective factor for isolating Brettanomyces/Dekkera yeast genera. Other secondary selective factors (selective carbon sources, sorbic acid and ethanol as a microbicide agent) may be used successfully to eliminate potential false positivities; however, they slow growth and delay the time to obtain results.

cDNA cloning of Batis maritima methyl chloride transferase and purification of the enzyme

Methyl chloride transferase catalyzes the synthesis of methyl chloride from S-adenosine-l-methionine and chloride ion. This enzyme has been purified 2,700-fold to homogeneity from Batis maritima, a halophytic plant that grows abundantly in salt marshes. The purification of the enzyme was accomplished by a combination of ammonium sulfate fractionation, column chromatography on Sephadex G100 and adenosine-agarose, and TSK-250 size-exclusion HPLC. The purified enzyme exhibits a single band on SDS/PAGE with a molecular mass of approximately 22.5 kDa. The molecular mass of the purified enzyme was 22,474 Da as determined by matrix-associated laser desorption ionization mass spectrometry. The methylase can function in either a monomeric or oligomeric form. A 32-aa sequence of an internal fragment of the methylase was determined (GLVPGCGGGYDVVAMANPER FMVGLDIXENAL, where X represents unknown residue) by Edman degradation, and a full-length cDNA of the enzyme was obtained by rapid amplification of cDNA ends–PCR amplification of cDNA oligonucleotides. The cDNA gene contains an ORF of 690 bp encoding an enzyme of 230 aa residues having a predicted molecular mass of 25,761 Da. The disparity between the observed and calculated molecular mass suggests that the methylase undergoes posttranslational cleavage, possibly during purification. Sequence homologies suggest that the B. maritima methylase defines a new family of plant methyl transferases. A possible function for this novel methylase in halophytic plants is discussed.