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Removing ink stains from the pages of ancient and valuable books is a very challenging and sometimes impossible task. Only in some circumstances, restorers are able to improve the appearance of an ink-stained page by lightening the spots using an ink eradicator. This paper reports on an approach for the removal of ink stains from a 17th century book using a combination of two commercial houseware products, the rust remover for textile and bleach. The products were chosen on the basis of their active ingredients such as hydrofluoric acid (HF), which facilitates the removal of metal ions contained in the inks (such as iron and chromium) and sodium hypochlorite (NaClO), known for its whitening abilities. The products were first tested by direct application to one of the several stained pages as a control experiment. The ink stain was successfully removed from the book, but by SEM analysis the page results in a clear detachment of the cellulose fibers from the paper pulp, which reflect a significant change in the paper fine structure. Moreover, the mixing of chemicals occurring during this procedure generated toxic vapors and the entire protocol could only be performed under a chemical fume hood. A new procedure was developed to mitigate these negative effects. Each of the two commercial products was dispersed in a 2% agarose solution shortly before its gelification and the two gels thus obtained were applied consecutively on the surface of the paper to be cleaned. The results showed an effective removal of the ink stain from treated page, avoiding irreparable damage to the paper structure and improving the working conditions of the restorers. Hence, the proposed gel cleaning procedure offers three main advantages: i) a simple and practical tool for effective removal of metallic ink stains from the paper surface; ii) reduction of damage caused by aggressive reagents (HF and NaClO) contained in cleaning products for a better conservation of paper fibers; iii) a great decrease of the risk of accidentally exposing the operators to harmful toxic vapor (produced by accidental mixing of aforementioned chemical reagents). [ABSTRACT FROM AUTHOR]

Biofilm is accountable for nosocomial infections and chronic illness, making it a serious economic and public health problem. Staphylococcus epidermidis, thanks to its ability to form biofilm and colonize biomaterials, represents the most frequent causative agent involved in biofilm-associated infections of medical devices. Therefore, the research of new molecules able to interfere with S. epidermidis biofilm formation has a remarkable interest. In the present work, the attention was focused on Pseudomonas sp. TAE6080, an Antarctic marine bacterium able to produce and secrete an effective antibiofilm compound. The molecule responsible for this activity was purified by an activity-guided approach and identified by LC-MS/MS. Results indicated the active protein was a periplasmic protein similar to the Pseudomonas aeruginosa PAO1 azurin, named cold-azurin. The cold-azurin was recombinantly produced in E. coli and purified. The recombinant protein was able to impair S. epidermidis attachment to the polystyrene surface and effectively prevent biofilm formation. [ABSTRACT FROM AUTHOR]

Polyethylene (PE) is high molecular weight synthetic polymer, very hydrofobic and hardly biodegradable. To increase polyethylene bio-degradability it is very important to find microorganisms that improve the PE hydrophilic level and/or reduce the length of its polymeric chain by oxidation. In this study, we isolated Cladosporium halotolerans , a fungal species, from the gastric system of Galleria mellonella larvae. Here, we show that C. halotolerans grows in the presence of PE polymer, it is able to interact with plastic material through its hyphae and secretes enzymes involved in PE degradation. [ABSTRACT FROM AUTHOR]

The development of new approaches to prevent microbial surface adhesion and biofilm formation is an emerging need following the growing understanding of the impact of biofilm-related infections on human health. Staphylococcus epidermidis, with its ability to form biofilm and colonize biomaterials, represents the most frequent causative agent involved in infections of medical devices. In the research of new anti-biofilm agents against S. epidermidis biofilm, Antarctic marine bacteria represent an untapped reservoir of biodiversity. In the present study, the attention was focused on Psychrobacter sp. TAE2020, an Antarctic marine bacterium that produces molecules able to impair the initial attachment of S. epidermidis strains to the polystyrene surface. The setup of suitable purification protocols allowed the identification by NMR spectroscopy and LC-MS/MS analysis of a protein–polysaccharide complex named CATASAN. This complex proved to be a very effective anti-biofilm agent. Indeed, it not only interferes with cell surface attachment, but also prevents biofilm formation and affects the mature biofilm matrix structure of S. epidermidis. Moreover, CATASAN is endowed with a good emulsification activity in a wide range of pH and temperature. Therefore, its use can be easily extended to different biotechnological applications. [ABSTRACT FROM AUTHOR]

Lipopolysaccharide (LPS) is an essential component of the outer membrane (OM) in most gram-negative bacteria, and its structure and biosynthetic pathway are well known. Nevertheless, the mechanisms of transport and assembly of this molecule at the cell surface are poorly understood. The inner membrane (IM) transport protein MsbA is responsible for flipping LPS across the IM. Additional components of the LPS transport machinery downstream of MsbA have been identified, including the OM protein complex LptD/LptE (formerly Imp/RlpB), the periplasmic LptA protein, the IM-associated cytoplasmic ATP binding cassette protein LptB, and LptC (formerly YrbK), an essential IM component of the LPS transport machinery characterized in this work. Here we show that depletion of any of the proteins mentioned above leads to common phenotypes, including (i) the presence of abnormal membrane structures in the periplasm, (ii) accumulation of de novo-synthesized LPS in two membrane fractions with lower density than the OM, and (iii) accumulation of a modified LPS, which is ligated to repeating units of colanic acid in the outer leaflet of the IM. Our results suggest that LptA, LptB, LptC, LptD, and LptE operate in the LPS assembly pathway and, together with other as-yet-unidentified components, could be part of a complex devoted to the transport of LPS from the periplasmic surface of the IM to the OM. Moreover, the location of at least one of these five proteins in every cellular compartment suggests a model for how the LPS assembly pathway is organized and ordered in space.