Thermal hydrolysis of sewage sludge: Improvement in biogas generation and prediction of global warming potential.

Anaerobic digestion (AD) is a prominent treatment method for the sludge produced from sewage treatment plants. Poor solid reduction and longer retention time are the main drawbacks of AD. Thermal hydrolysis (TH) is a potential pretreatment method for solubilization of sewage sludge (SS) solids thereby improving biogas production during AD post-treatment. In this study, the SS sample (total solids = 1.75 wt% and total chemical oxygen demand (COD) = 15,450 mg L-1) was subjected to TH pretreatment (temperature = 140-180°C and reaction time = 60 minutes) in a 0.7-L capacity stainless-steel high-pressure reactor. At a reaction temperature of 180°C, the maximum solid solubilization (total dissolved solids = 4652 mg L-1) and improved dewaterability (time to filter = 4.7 s.L g-1) were observed. The biochemical methane potential test results showed almost doubling of methane generation from 145 to 284 mL gCOD-1 after TH pretreatment at 180°C. The life cycle assessment approach was used to compare various SS treatment and disposal scenarios, two of which included hydrothermal pretreatment. The scenarios involving hydrothermal pretreatments showed the least global warming potential.

Concomitant Guillain Barre Syndrome and Transverse Myelitis as Initial Neuropsychiatric Manifestation in a Case of Lupus: A Diagnostic Quandary.

Neuropsychiatric manifestations of systemic lupus erythematosus are varied. Presently nineteen in number, they are classified as whether affecting the central or the peripheral compartments of the nervous system. Its diagnosis however remains difficult, more so when two or more of the syndromes are found concomitantly in the same patient and when they occur in absence of the more classical rash, serositis, and haematological manifestations. We present a case of lupus where myelopathy as well as demyelination existed simultaneously as the initial neurologic manifestation.

Characterization of M. tuberculosis SerB2, an essential HAD-family phosphatase, reveals novel properties.

M. tuberculosis harbors an essential phosphoserine phosphatase (MtSerB2, Rv3042c) that contains two small- molecule binding ACT-domains (Pfam 01842) at the N-terminus followed by the phosphoserine phosphatase (PSP) domain. We found that exogenously added MtSerB2 elicits microtubule rearrangements in THP-1 cells. Mutational analysis demonstrates that phosphatase activity is co-related to the elicited rearrangements, while addition of the ACT-domains alone elicits no rearrangements. The enzyme is dimeric, exhibits divalent metal- ion dependency, and is more specific for l- phosphoserine unlike other classical PSPases. Binding of a variety of amino acids to the ACT-domains influences MtSerB2 activity by either acting as activators/inhibitors/have no effects. Additionally, reduced activity of the PSP domain can be enhanced by equimolar addition of the ACT domains. Further, we identified that G18 and G108 of the respective ACT-domains are necessary for ligand-binding and their mutations to G18A and G108A abolish the binding of ligands like l- serine. A specific transition to higher order oligomers is observed upon the addition of l- serine at ∼0.8 molar ratio as supported by Isothermal calorimetry and Size exclusion chromatography experiments. Mutational analysis shows that the transition is dependent on binding of l- serine to the ACT-domains. Furthermore, the higher-order oligomeric form of MtSerB2 is inactive, suggesting that its formation is a mechanism for feedback control of enzyme activity. Inhibition studies involving over eight inhibitors, MtSerB2, and the PSP domain respectively, suggests that targeting the ACT-domains can be an effective strategy for the development of inhibitors.