Unveiling the genomic potential of a novel thermostable glycoside hydrolases producing Neobacillus sedimentimangrovi UE25.

Genetic and enzymatic potential of Neobacillus sedimentimangrovi has not been assembled to date. Here, we report a high-quality genome assembly of thermophilic bacterium Neobacillus sedimentimangrovi UE25 using Illumina Hi-seq 2500. The strain was isolated from a crocodile pond Manghopir, Karachi, Pakistan.

Wild Halophytic Biomass Saccharification by Bacterial Enzyme Cocktail.

Biofuel derived from halophytic biomass is getting attention owing to the concerns of energy versus food crisis. The disadvantages associated with edible bioenergy resources necessitate the need to explore new feedstocks for sustainable biofuel production. In this study, biomass from locally available abundant halophytes (, , , and ) was screened for saccharification by an enzyme cocktail composed of cellulase, xylanase, and pectinase from UE10 and UE27, UE25, UE1, and MH 1.

Banana Peels: A Promising Substrate for the Coproduction of Pectinase and Xylanase from MS16.

Banana peels (BP), an under-utilized waste material, was studied for the production of xylanase and pectinase by MS16. The factors affecting the co-production of both the enzymes were separately studied for their influence under submerged (Smf) and solid-state fermentation (SSF) of BP. The strain was cultivated in the presence of mineral salt (MS) solution containing BP powder as a sole source of carbon and physical and nutritional factors varied to observe the change in the enzyme titers.

Screening for toxigenic Escherichia coli in stool samples of diarrhoeal patients by polymerase chain reaction.

Escherichia coli (E. coli) are normal flora of the intestines of most animals, including humans. Most strains are harmless and beneficial to host by preventing the establishment of pathogenic bacteria within the intestine.

Purification and characterization of novel α-amylase from Bacillus subtilis KIBGE HAS.

Purification of extracellular α-amylase from Bacillus subtilis KIBGE HAS was carried out by ultrafiltration, ammonium sulfate precipitation and gel filtration chromatography. The enzyme was purified to homogeneity with 96.3-fold purification with specific activity of 13011 U/mg.