Welcome to the inaugural Issue of Pakistan BioMedical Journal

Firstly, I would like to welcome all the readers, authors, editorial team and management of Pakistan Biomedical Journal (PBMJ) to this new journal in Biomedical Sciences. It is an intenational peer-reviewed, open-access journal that merges the basic and clinical research for the better outcome in terms of diagnosis and therapeutics. This approach will update and upgrade the existing knowledge among the researchers and clinicians, regarding the patient care and practice as well as understanding of underlying mechanisms of diseases. The ultimate beneficiary is patient and community as a whole. PBMJ is led by an outstanding Editorial Board comprising of national and international members with multidisciplinary research background. Our goal is to promote the basic and clinical research, health and disease perspectives. We receive original studies, review articles, case reports, systemetic reviews on medical, biomedical, basic and therapeutic research. We welcome scientific contributions from all over the world. It is the need and demand of the recent world scenario to focus on biomedical research. In the current world, basic and medical science cannot be considered as two separate and independent entities. There should be coherent efforts to unveil the basic understandings of pathologies at physiological, cellular and molecular level. Furthermore, the therapeutic strategies should also be explored on regional and global levels, by keeping in mind the different genetic makeups and considering the individual identities. It leads to the field of ‘personalized medicine’. There are many other recent therapeutic regimens such as regenerative medicine, exosomes, gene silencing and gene editing technologies. The world has also advanced in diagnostic modalities. Much focus has been emphasized on rapidness, accuracy and cost-effectiveness of these techniques. Imaging, scanning, histopathological, biochemical and hematological techniques have been much advanced than before. World has been changing rapidly in medical profession. Hence, it is important to be aware of these advancements worldwide and also to share the health related researches at local level. We hope this new journal will be a good addition in this perspective of sharing the recent knowledge, advancements and create awareness among masses.

Production and Characterization of Pectinases by Aspergillus Niger for Industrial Use

Two hundred and sixteen fungal strains were isolated from two hundred fifty soil samples collected from different localities of Punjab and subjected to screening for their pectinolytic ability using submerged fermentation. One hundred and fifty one pectinolytic strains were subjected to secondary screening and isolate IIB-13 gave the maximum pectinase yield (10.78±0.45U/ml/min) and identified as Aspergillus niger using morphological characteristics. Random mutagenesis (physical and chemical) was used to improve the pectinolytic activity of strain IIB-13. Nitrous acid mutant H-97 resulted in three fold increase (32.16 + 0.05U/ml/min) in pectinase production. This H-97strain was further subjected to optimization of media, carbon and nitrogen sources, temperature and pH. Maximum pectinase (37.01±0.11 U/ml/min) was produced using medium containing K2HPO4 (4.0 g), yeast extract (0.6 g), KH2PO4 (1.28 g), (NH4)2SO4 (2.0 g), MgSO4 (1.1 g) and pectin (10 g) per 1.0 L of distilled water at pH and temperature (7.0 and 30°C) respectively after 60 hours of fermentation. Fermenter studies (7.5 L) resulted in increased pectinase activity (40.31±0.07 U/ml/min) with decreased incubation time of 48 h using 1% inoculums with optimized reaction conditions i.e. temperature (30°C), pH (07), agitation (200 rpm) and aeration (1vvm). Fermentation kinetics was applied to validate the results. The crude enzyme was subjected to purification by applying ammonium sulfate precipitation and Ion exchange chromatography which resulted in 44.20 % yield with increased activity i.e. 75.18±0.04 U/mg. Km value of 2.30 mg/ml using pectin as substrate showed its maximum specificity for the enzyme. Activation energy (Ea) i.e. -28.95 KJ/mol and enthalpy of activation (ΔH) i.e. -26.73 KJ/mol were calculated employing thermodynamic studies. Characterization of enzyme revealed catalytic activity optimum temperature and pH as 25°C and pH 7. The enzymes catalytic activity was observed to be reduced by some heavy metals such as Hg2+, Pb2+, Cu+ and Cd2+.