Serratia sp. scl1: isolation of a novel thermostable lipase producing microorganism which holds industrial importance.

Lipase being a hydrolysable enzyme plays a major role in serving various purposes of the industries. Thus, it is very important to have a sustainable and efficient source of this enzyme. In this present study, several microorganisms were isolated from medicinal effluent of a pharmaceutical industry that could produce efficient lipase activity. Among these isolates, a designated strain scl1 was isolated and based on the molecular and biochemical characterisation was tentatively assigned to the genus Serratia. Preliminary studies confirmed the strain scl1 was found to exhibit the highest production of lipase at a temperature and pH of 35 °C and 7, respectively under the incubation for 48 h. Further, the lipase activity was measured by following spectrophotometric method using pNPP as the substrate in which the Km and Vmax of the crude enzyme was found to be 3.349 × 10-3 M and 5.68 × 10-1 unit/mL, respectively. The extracellular crude lipase was found to show a temperature and pH optima of 75 °C and 8, respectively which gave a strong indication that the enzyme appeared to be highly thermostable. This study revealed the strain scl1 is able to produce a thermostable lipase which can meet the needs of the modern-day industrialization techniques. However, more work is required to purify the enzyme and get it ready for commercial applications.

Exposure to Spectracide® causes behavioral deficits in Drosophila melanogaster: Insights from locomotor analysis and molecular modeling.

This study was focused on gaining insights into the mechanism by which the herbicide- Spectracide®, induces oxidative stress and alters behavior in Drosophila melanogaster. Exposure to Spectracide® (50%) significantly (p < 0.05) reduced the negative geotaxis response, jumping behavior and dampened locomotor activity rhythm in adult flies compared to non-exposed flies. Protein carbonyl levels indicative of oxidative damage increased significantly coupled with down-regulation of Sniffer gene expression encoding carbonyl reductase (CR) and its activity in Spectracide®-exposed flies. In silico modeling analysis revealed that the active ingredients of Spectracide® (atrazine, diquat dibromide, fluazifop-p-butyl, and dicamba) have significant binding affinity to the active site of CR enzyme, with atrazine having comparatively greater affinity. Our results suggest a mechanism by which ingredients in Spectracide® induce oxidative damage by competitive binding to the active site of a protective enzyme and impair its ability to prevent damage to proteins thereby leading to deficits in locomotor behavior in Drosophila.

Pharmacophore modeling coupled with molecular dynamic simulation approach to identify new leads for meprin-ß metalloprotease.

Human meprin beta metalloprotease, a small subgroup of the astacin family, is a potent drug target for the treatment of several disorders such as fibrosis, neurodegenerative disease in particular Alzheimer and inflammatory bowel diseases. In this study, a ligand-based pharmacophore approach has been used for the selection of potentially active compounds to understand the inhibitory activities of meprin-ß by using the sulfonamide scaffold based inhibitors. Using this dataset, a pharmacophore model (Hypo1) was selected on the basis of a highest correlation coefficient (0.959), lowest total cost (105.89) and lowest root mean square deviation (1.31 Å) values. All the pharmacophore hypotheses generated from the candidate inhibitors comprised four features: two hydrogen-bond acceptor, one hydrogen-bond donor and one zinc binder feature. The best validated pharmacophore model (Hypo1) was used for virtual screening of compounds from several databases. The selective hit compounds were filtered by drug likeness property, acceptable ADMET profile, molecular docking and DFT study. Molecular dynamic simulations with the final 10 hit compounds revealed that a large number of non-covalent interactions were formed with the active site and specificity sub-pockets of the meprin beta metalloprotease. This study assists in the development of the new lead molecules as well as gives a better understanding of their interaction with meprin-ß.