Colimetry of marine waters off Fortaleza (Ceará State, Brazil) and detection of enteropathogenic Escherichia coli strains.

Bacteriological analyses of seawater from three main beaches in Fortaleza, Brazil were performed during 1997. Thirty-six samples per beach were collected for a total of 108 samples. For Meireles Beach, 44% of the samples had MPN total coliforms values of at least 1100 or over 2400/100 ml, followed by Formosa and Diários beaches showing lower counts. For fecal coliforms the highest numbers were demonstrated for Formosa, followed by Meireles and Diários beaches in this descending order: 13.0%, 11.1% and 8.3%, respectively. Escherichia coli strains were identified in 76.8% of the 108 samples. Among 295 strains of E. coli, 21 belonged to serogroups O25, O26, O91, O112, O119, O158 and O164. Strains from serogroup O26 were tested using PCR, ELISA and Vero cells to detect Verotoxins VT1 and VT2 and all strains were negative. No LT and ST, as determined by ELISA and suckling mice assays, were detected among the 295 strains. All strains of E. coli were sensitive to ampicillin, cephalothin, gentamicin, tetracycline, sulfametox-trimethoprim, chloramphenicol and ciprofloxacin. Although the E. coli strains were not toxigenic, their presence in high numbers could be of public health significance.     

DMSO enhanced conformational switch of an interfacial enzyme

Interfacial proteins function in unique heterogeneous solvent environments, such as water–oil interfaces. One important example is microbial lipase, which is activated in an oil‐water emulsion phase and has many important enzymatic functions. A unique aprotic dipolar organic solvent, dimethyl sulfoxide (DMSO), has been shown to increase the activity of lipases, but the mechanism behind this enhancement is still unknown. Here, all‐atom molecular dynamics simulations of lipase in a binary solution were performed to examine the effects of DMSO on the dynamics of the gating mechanism. The amphiphilic α5 region of the lipase was a focal point for the analysis, since the structural ordering of α5 has been shown to be important for gating under other perturbations. Compared to the closed‐gorge ensemble in an aqueous environment, the conformational ensemble shifts towards open‐gorge structures in the presence of DMSO solvents. Increased width of the access channel is particularly prevalent in 45% and 60% DMSO concentrations (w/w). As the amount of DMSO increases, the α5 region of the lipase becomes more α‐helical, as we previously observed in studies that address water–oil interfacial and high pressure activation. We believe that the structural ordering of α5 plays an essential role on gating and lipase activity.