Linkage disequilibrium block single-nucleotide polymorphisms in FTO alpha ketoglutarate dependent dioxygenase gene inference with breast cancer and Type II diabetes in Pakistani female population.

Breast Cancer and Diabetes Mellitus are top ranked non-communicable life threatening diseases concerned in South Asia. The growing scientific clues witness the involvement of genetic variations which readily serve as risk factors for the disease onset. Comprehending the association of genetic predictors and risk factors in the conserved genome regions can help reveal underlying disease genetics and identify the sustained druggable targets.

Thermodynamics, kinetics and optimization of catalytic behavior of polyacrylamide-entrapped carboxymethyl cellulase (CMCase) for prospective industrial use.

In the current study, kinetic and thermodynamic parameters of free and polyacrylamide-immobilized CMCase were analyzed. The maximum immobilization yield of 34 ± 1.7% was achieved at 11% acrylamide.

Single step immobilization of CMCase within agarose gel matrix: Kinetics and thermodynamic studies.

In the current study, CMCase from Bacillus licheniformis KIBGE-IB2 was immobilized within the matrix of agarose gel through entrapment technique. Maximum immobilization yield (%) of the enzyme was obtained when 2.0 % agarose was used.

Encapsulation of pectinase within polyacrylamide gel: characterization of its catalytic properties for continuous industrial uses.

Pectinase as a biocatalyst play a significant role in food and textile industries. In this study, the pectinase was immobilized by encapsulation within polyacrylamide gel to enhance its catalytic properties and ensure the reusability for continuous industrial processes. 9.

Utilization of different polymers for the improvement of catalytic properties and recycling efficiency of bacterial maltase.

Current study deals with the comparative study related to immobilization of maltase using synthetic (polyacrylamide) and non-synthetic (calcium alginate, agar-agar and agarose) polymers via entrapment technique. Polyacrylamide beads were formed by cross-linking of monomers, agar-agar and agarose through solidification while alginate beads were prepared by simple gelation. Results showed that the efficiency of enzyme significantly improved after immobilization and among all tested supports agar-agar was found to be the most promising and biocompatible for maltase in terms of immobilization yield (82.

REPORT- Role of metal ions on the catalytic efficiency of dextran hydrolyzing biocatalyst.

Hydrothermal spring isolate Bacillus megaterium KIBGE-IB31was utilized to produce dextranase. Enzyme was partially purified up to 11.8 fold after dialysis.

A comparative study on degradation of complex malathion organophosphate using of Escherichia coli IES-02 and a novel carboxylesterase.

Malathion organophosphates considered as the major constituent of herbicides, pesticides and insecticides. Extensively used in agricultural, horticultures and for numerous household applications contributes to precedence organic pollutants leading antagonistic effects on human health and environment. Therefore detoxification of malathion from contaminated site is of general interest.

Maltose deterioration approach: Catalytic behavior optimization and stability profile of maltase from KIBGE-IB4.

Maltase is an economically valuable enzyme that is used to catalyze the hydrolytic process of maltose and yields d-glucose as a product. In this study, the catalytic behavior of maltase was optimized under various physicochemical condition. Results indicated that bacterial maltase exhibited maximum catalytic activity at 45 °C and pH-6.

Improvement of catalytic properties of starch hydrolyzing fungal amyloglucosidase: Utilization of agar-agar as an organic matrix for immobilization.

In this study, amyloglucosidase was immobilized within agar-agar through entrapment technique for the hydrolysis of soluble starch. Enzymatic activities of soluble and entrapped amyloglucosidase were compared using soluble starch as a substrate. Partially purified enzyme was immobilized and maximum immobilization yield (80%) was attained at 40 gL of agar-agar.

Purification and catalytic behavior optimization of lactose degrading β-galactosidase from .

The β-galactosidase is an industrially valuable enzyme and used to hydrolyze the lactose into glucose and galactose. Considering the broad utility profile in food industry, β-galactosidase from was purified and characterized in term of its catalytic properties and stability. It displayed highest catalytic efficiency at 60 °C after 10.

Bioprospecting of indigenous resources for the exploration of exopolysaccharide producing lactic acid bacteria.

Exploration of biodiversity lead towards the discovery of novel exopolysaccharide (EPS) producing microbes that have multiple applications. The safety compatibility status of lactic acid bacteria (LAB) makes it an attractive candidate for the production of EPS in industries. Therefore, new bacterial isolates are continuously being identified from different habitats.

Screening, purification and characterization of thermostable, protease resistant Bacteriocin active against methicillin resistant Staphylococcus aureus (MRSA).

Background: The emergence of serious issues of multidrug resistance in the past few years have enforced the use of bacteriocins for combating infections. Threat posed to public health by various multidrug resistant (MDR) organisms can be resolved by discovering new antimicrobial proteins with broad spectrum of inhibition.

Results: In the current study, Bacteriocin (BAC-IB17) produced by Bacillus subtilis KIBGE-IB17 is found to be effective against different strains of methicillin resistant Staphylococcus aureus (MRSA).

Characterization of cross-linked amyloglucosidase aggregates from Aspergillus fumigatus KIBGE-IB33 for continuous production of glucose.

Current research deals with immobilization of amyloglucosidase through carrier-free approach using cross-linking strategy. Cross-linked amyloglucosidase aggregates (CLAAs) with aggregation yield of 94% were prepared in 04 h by incorporating 40% ammonium sulfate and 1.5% glutaraldehyde in enzyme solution.

Characterization and interplay of bacteriocin and exopolysaccharide-mediated silver nanoparticles as an antibacterial agent.

Metallic nanoparticles have a substantial scientific interest because of their distinctive physicochemical and antimicrobial properties and the emergence of multidrug resistant pathogens could unlock the potential of nanoparticles to combat infectious diseases. The aim of the current study is to enhance the antibacterial potential of purified bacteriocin by combining bacteriocin and antibacterial silver nanoparticles (AgNPs). Hence, the interaction of natural antimicrobial compounds and antibacterial nanoparticles can be used as a potential tool for combating infectious diseases.

Enhanced biosynthesis of dextransucrase: A multivariate approach to produce a glucosyltransferase for biocatalysis of sucrose into dextran.

The current study reported the statistically designed experimental method to enhance the biocatalytic efficacy of dextransucrase from Weissella confusa. Various environmental and nutritional parameters were optimized using multiple responses under submerged fermentation environment. Statistical models were constructed to screen the influence of nine factors on the biocatalysis of dextransucrase.

Agar-agar immobilization: An alternative approach for the entrapment of protease to improve the catalytic efficiency, thermal stability and recycling efficiency.

The catalytic performance of an immobilized enzyme could be enhanced by using entrapment technique. In this contemporary study agar-agar, a natural polysaccharide, is subjected to entrap serine-protease produced by Aspergillus niger KIBGE-IB36. The results revealed that maximum enzymatic activity was attained when 3.

Utilization of agro waste pectin for the production of industrially important polygalacturonase.

In the present study, a variety of agro-industrial wastes have been utilized for meaningful purpose to produce valuable biocatalyst. All wastes used were low cost and easily accessible while, some available throughout the year. A number of bacterial strains isolated from rotten fruits and vegetables were screened for the production of industrially important polygalacturonase (PGase) using pectin present in these agro-industrial wastes.

Enzymatic and acidic degradation of high molecular weight dextran into low molecular weight and its characterizations using novel Diffusion-ordered NMR spectroscopy.

Low molecular weight fractions were derived from native high molecular weight dextran produced by Leuconostoc mesenteroides KIBGE-IB26. Structural characterization of native and low molecular weight fractions obtained after acidic and enzymatic hydrolysis was done using FTIR and NMR spectroscopy. The molecular weight was estimated using Diffusion Ordered NMR spectroscopy.

Role of two polysaccharide matrices on activity, stability and recycling efficiency of immobilized fungal amyloglucosidase of GH15 family.

Current study deals with immobilization of amyloglucosidase using two different strategies (entrapment and covalent binding). Chitosan beads were prepared using neutralization method while alginate beads were synthesized by simple gelation. Results of this study showed that percent recovery of amyloglucosidase after covalent binding was 85% however in case of entrapment it was 66%.

Production of α-1,4-glucosidase from Bacillus licheniformis KIBGE-IB4 by utilizing sweet potato peel.

In the current study, sweet potato peel (Ipomoea batatas) was observed as the most favorable substrate for the maximum synthesis of α-1,4-glucosidase among various agro-industrial residues. Bacillus licheniformis KIBGE-IB4 produced 6533.0 U ml of α-1,4-glucosidase when growth medium was supplemented with 1% dried and crushed sweet potato peel.

Polyacrylamide Gel-Entrapped Maltase: An Excellent Design of Using Maltase in Continuous Industrial Processes.

Bacterial maltase catalyzes the hydrolysis of maltose and is known as one of the most significant hydrolases. It has several applications in different industrial processes but widely used in food fermentation technology and alcohol production. In the current study, entrapment technique was comprehensively examined using polyacrylamide gel as a matrix support to improve the stability and catalytic efficiency of maltase for continuous use.

Role of nutrients and environmental conditions for the production of dextransucrase from L. mesenteroides KIBGE-IB26.

The bacterial strains capable of producing dextransucrase enzyme were isolated from different fruits and vegetables sources. In primary screening, five strains were selected on the basis dextransucrase production and among them L. mesenteroides KIBGE- IB26 isolated from bottle gourd (Lagenaria Vulgaris) was selected for further studies.

Morphological and molecular based identification of pectinase producing from rotten vegetable.

Pectinase catalyzed the degradation of pectin substances and has been used in various biotechnological industries. In the current study, 23 bacterial strains were isolated from rotten vegetables, soil and air. The isolated bacterial strains were qualitatively screened for pectinase production on pectin agar medium and only three strains HR 4, HR 21 and HR 23 were observed to produce extracellular pectinase.