Diagnostic accuracy of B-scan in predicting retinoblastoma in children, taking Magnetic Resonance Imaging of orbits as gold standard.

The objective of this study was to determine the diagnostic accuracy of B-scan in predicting retinoblastoma (Rb) taking Magnetic Resonance Imaging (MRI) as a gold standard. A cross-sectional validation study was conducted in the Radiology Department of Fauji Foundation Hospital from May 20 to Nov 20, 2017. Children fulfilling the inclusion criteria were selected after informed consent and detailed history was taken for investigation of Rb. B-scan of both eyes was done using 7.5-10 MHz probe, followed by MRI of both eyes in the same patients using 1.5 Tesla MRI machine with the help of qualified MRI technicians. Data analysis was done by SPSS version 16.0. The diagnostic accuracy, sensitivity, specificity, PPV and NPV of B-scan in prediction of Rb as compared to MRI was 90.45%, 82.28%, 90.54% and 90.28% respectively. The study concluded that diagnostic accuracy of B-scan as compared to MRI is substantial in Retinoblastoma.

Immobilization of pectin depolymerising polygalacturonase using different polymers.

Polygalacturonase catalyses the hydrolysis of pectin substances and widely has been used in food and textile industries. In current study, different polymers such as calcium alginate beads, polyacrylamide gel and agar-agar matrix were screened for the immobilization of polygalacturonase through entrapment technique. Polyacrylamide gel was found to be most promising one and gave maximum (89%) immobilization yield as compared to agar-agar (80%) and calcium alginate beads (46%). The polymers increased the reaction time of polygalacturonase and polymers entrapped polygalacturonases showed maximum pectinolytic activity after 10 min of reaction as compared to free polygalacturonase which performed maximum activity after 5.0 min of reaction time. The temperature of polygalacturonase for maximum enzymatic activity was increased from 45°C to 50°C and 55°C when it was immobilized within agar-agar and calcium alginate beads, respectively. The optimum pH (pH 10) of polygalacturonase was remained same when it was immobilized within polyacrylamide gel and calcium alginate beads, but changed from pH 10 to pH 9.0 after entrapment within agar-agar. Thermal stability of polygalacturonase was improved after immobilization and immobilized polygalacturonases showed higher tolerance against different temperatures as compared to free enzyme. Polymers entrapped polygalacturonases showed good reusability and retained more than 80% of their initial activity during 2nd cycles.

Plasmid borne BAC-IB17: Localization of a potential antibacterial positive marker (Bac+) encoded broad inhibitory spectrum bacteriocin.

Production of antimicrobial compounds is considered as ubiquitous anti-competitor strategy in bacterial ecosystem. Bacteriocins are heterogeneous; highly specific and efficient anti-competitor agents and the gene responsible for the production of bacteriocins mostly exist in an autosomal state and associated with plasmids. BAC-IB17 is a broad spectrum bacteriocin and its production was observed at different stages of the growth cycle from Bacillus subtilis KIBGE-IB17. Growth kinetics of B. subtilis KIBGE-IB17 along with the production of BAC-IB17 showed that it exhibited secondary metabolite kinetics. Plasmid curing technique revealed that the gene responsible for the bacteriocinogenecity in B. subtilis KIBGE-IB17 was located on the plasmid of the bacterium. Overlay method also demonstrated the plasmid-mediated bacteriocinogenesis of the isolated colonies. With the advancement in genomics and proteomics, the plasmid borne BAC-IB17 can play a significant role in the transfer of bacteriocinogenic factor to other incompetent cells and also in the maintenance of plasmid in bacterial population.

Isolation and characterization of different strains of Bacillus licheniformis for the production of commercially significant enzymes.

Utilization of highly specific enzymes for various industrial processes and applications has gained huge momentum in the field of white biotechnology. Selection of a strain by efficient plate-screening method for a specific purpose has also favored and boosted the isolation of several industrially feasible microorganisms and screening of a large number of microorganisms is an important step in selecting a potent culture for multipurpose usage. Five new bacterial isolates of Bacillus licheniformis were discovered from indigenous sources and characterized on the basis of phylogeny using 16S rDNA gene analysis. Studies on morphological and physiological characteristics showed that these isolates can easily be cultivated at different temperatures ranging from 30°C to 55°C with a wide pH values from 3.0 to 11.0 All these 05 isolates are salt tolerant and can grow even in the presences of high salt concentration ranging from 7.0 to 12.0%. All these predominant isolates of B. licheniformis strains showed significant capability of producing some of the major industrially important extracellular hydrolytic enzymes including α-amylase, glucoamylase, protease, pectinase and cellulase in varying titers. All these isolates hold great potential as commercial strains when provided with optimum fermentation conditions.

Dextranase: hyper production of dextran degrading enzyme from newly isolated strain of Bacillus licheniformis.

Dextranase, 6-alpha-D-glucan 6-glucanohydrolase catalyzes the degradation of dextran (polymer of D-glucose) in to low molecular weight fractions. Dextranolytic bacterial strains were isolated from various natural sources and plate assay methods were developed for screening of highest extracellular dextranase producing isolate. Bacillus licheniformis, identified on the basis of taxonomic characterization was subjected to UV radiation and highest enzyme producing mutant obtained led to 7 times more dextranase production than wild. Optimization of major physico-chemical parameters affecting enzyme production; including medium composition, pH, cultivation time and temperature revealed that maximum enzyme production was obtained in a self designed medium (pH 6.0) containing 1% Dextran 5000 Da, after 24 h culture incubation at 37 °C. Dextranase reported in this study is of great commercial importance as it is strictly inducible in nature and B. licheniformis being non-pathogenic removes the safety concerns associated with production of dextran fractions for clinical and pharmaceutical usage.