Alteromonas hispanica sp. nov., a polyunsaturated-fatty-acid-producing, halophilic bacterium isolated from Fuente de Piedra, southern Spain.

Strain F-32T, which produces exopolysaccharides and contains polyunsaturated fatty acids, was isolated from a hypersaline water sample collected from Fuente de Piedra (southern Spain). Phylogenetic analyses indicated conclusively that the strain in question belonged to the genus Alteromonas. Phenotypic tests showed that it could be assigned to the genus Alteromonas although it had a number of distinctive characteristics: it is moderately halophilic, growing best with 7.5-10 % w/v NaCl; it grows at 4 degrees C and produces H2S; it does not grow with d-cellobiose, d-fructose, d-galactose, d-glucose or lactose as sole sources of carbon and energy; and its fatty-acid profile is typical of Alteromonas but it also contains a large amount of an unusual acid with three double bonds [18 : 3omega6c (6, 9, 12); 5.01 %, w/v]. The major isoprenoid quinone is Q8. The DNA G+C content is 46.3 mol%. The phylogenetic, phenotypic and genetic properties of strain F-32T place it within a novel species, for which the name Alteromonas hispanica sp. nov. is proposed. The type strain is F-32T (=CECT 7067T=LMG 22958T).

Surface characterization of three marine bacterial strains by Fourier transform IR, X-ray photoelectron spectroscopy, and time-of-flight secondary-ion mass spectrometry, correlation with adhesion on stainless steel surfaces.

Adhesion of bacterial strains on solid substrates is likely related to the properties of the outer shell of the micro-organisms. Aiming at a better understanding and control of the biofilm formation in seawater, the surface chemical composition of three marine bacterial strains was investigated by combining Fourier transform IR spectroscopy, X-ray photoelectron spectroscopy (XPS), and time-of-flight secondary-ion mass spectrometry (ToF-SIMS). The D41 strain surface showed evidence of proteins, as deduced from the NH2 and NCO XPS and ToF-SIMS fingerprints; this strain was found to adhere to stainless steel, glass, or Teflon surfaces in a much higher quantity (2 orders of magnitude) than the two other ones, DA and D01. The latter are either enriched in COOH or sulfates, and this makes them more hydrophilic and less adherent to all substrates. Correlations with physicochemical properties and adhesion seem to demonstrate the role of the external layer composition, in particular the role of proteins more than that of hydrophobicity, on their adhesion abilities.

Purification and characterization of bifunctional alginate lyase from Alteromonas sp. strain no. 272 and its action on saturated oligomeric substrates.

A marine bacterium (strain No. 272) isolated from sea mud in Omura Bay produced an alginate lyase and was classified as an Alteromonas species. The enzyme was purified from the culture medium of the bacterium by DEAE-Cellulofine, Sephadex G-100 gel chromatography to an electrophoretically homogeneous state in the presence and absence of SDS. The molecular mass of the enzyme was 23 and 33.9 kDa on Sephadex G-100 column chromatography and SDS-polyacrylamide gel electrophoresis, respectively, with an isoelectric point of 3.8. The predominant secondary structure of the enzyme was found to be most likely beta-structure by circular dichroism. The enzyme was most active at pH 7.5-8.0 and stable around pH 5-11. The enzyme was more labile in Tris-HCI buffer (pH 7.0) to heat treatment, than in phosphate buffer (pH 7.0). No of metal ions significantly affected the enzyme activity. The enzyme acted on sodium alginate in an endo-type manner and on two components of alginate, poly-alpha1,4-L-guluronate and poly-beta1,4-D-mannuronate, as judged by routine ultraviolet assay (235 nm) and circular dichroic spectral changes of the substrates. However, the coexisting poly-alpha1,4-L-guluronate and poly-beta1,4-D-mannuronate apparently interacted with the enzyme in a competitive manner. Although the enzyme depolymerized alginate in an endo-type, it did not act on trimeric guluronate and mannuronate, but on the tetramers or more. The kinetic analyses showed that kcat/Km for each oligomer was larger for the guluronate oligomers than for the mannuronate ones, and that the subsite structure of the enzyme most likely consisted of six binding sites from the intrinsic reaction rate constant (kint) and intrinsic substrate binding constant (Kint).