Magnesium Sulfate Salt Solutions and Ices Fail to Protect Serratia liquefaciens from the Biocidal Effects of UV Irradiation under Martian Conditions.

The growth of Serratia liquefaciens has been demonstrated under martian conditions of 0.7 kPa (7 mbar), 0°C, and CO2-enriched anoxic atmospheres (Schuerger et al., 2013, Astrobiology 13:115-131), but studies into the survivability of cells under hypersaline conditions that are likely to be encountered on Mars are lacking. Serratia liquefaciens cells were suspended in aqueous MgSO4 solutions, or frozen brines, and exposed to terrestrial (i.e., 101.3 kPa, 24°C, O2/N2-normal atmosphere) or martian (i.e., 0.7 kPa, -25°C, CO2-anoxic atmosphere) conditions to assess the roles of MgSO4 and UV irradiation on the survival of S. liquefaciens. Four solutions were tested for their capability to attenuate martian UV irradiation in both liquid and frozen forms: sterile deionized water (SDIW), 10 mM PO4 buffer, 5% MgSO4, and 10% MgSO4. None of the solutions in either liquid or frozen forms provided enhanced protection against martian UV irradiation. Sixty minutes of UV irradiation reduced cell densities from 2.0 × 106 cells/mL to less than 10 cells/mL for both liquid and frozen solutions. In contrast, 3-4 mm of a Mars analog soil were sufficient to attenuate 100% of UV irradiation. Results suggest that terrestrial microorganisms may not survive on Sun-exposed surfaces on Mars, even if the cells are embedded in frozen martian brines composed of MgSO4. However, if dispersed microorganisms can be covered by only a few millimeters of dust or regolith, long-term survival is probable. Key Words: Hypobaria-Mars-Planetary protection-Brines. Astrobiology 17, 401-412.

Ser2 from Serratia liquefaciens L53: A new heat stable protease able to destabilize UHT milk during its storage.

The heat-stable protease Ser2 is secreted by the species Serratia liquefaciens, a psychrotrophic bacteria frequently found in raw milk. To understand the physicochemical modifications of casein micelles induced by Ser2 and to confirm its implication in UHT milk destabilization, the enzyme was purified and added to microfiltered raw milk before UHT treatment. UHT milk destabilization was investigated during 90days of storage. A visual destabilization appeared after 8days of storage with the presence of sediment. Zeta potential increase and formation of aggregates were observed during the storage. Using tandem mass spectrometry, numerous released peptides from the four caseins were identified at the end of storage. Caseins were hydrolyzed in the preferential order ß->αs1->κ->αs2. No specific peptidic hydrolysed bond was detected. The present study confirmed that the presence of the protease Ser2 in raw milk can be one of the main causes of UHT milk destabilization.