ڈاکٹر عبدالعلیم
ڈاکٹر عبدالعلیم سابق وائس چانسلر مسلم یونیورسٹی علی گڑھ اور صدر اردو بورڈ دہلی کی اچانک وفات سے پورے علمی حلقہ کو دکھ ہے، ان کے خیالات کچھ بھی رہے ہوں، لیکن وہ اپنی شرافت طبع اور مرنجان مرنج رویے کی وجہ سے ہر حلقہ میں پسند کئے جاتے تھے، جہاں رہے ان کا وزن اور وقار رہا، دارالمصنفین سے ان کے تعلقات برابر خوشگوار رہے، مسلم یونیورسٹی کے عربی اور اسلامیات کے شعبوں کو ترقی دینے میں بھی ان کی خدمات برابر یاد کی جائیں گی، وہ مسلم یونیورسٹی کے وائس چانسلر بہت ہی نازک دور میں بنائے گئے، ان پر نظر انتخاب ڈاکٹر ذاکر حسین خاں مرحوم کی پڑی تھی، جو ان کو بہت محبوب رکھتے تھے، انھوں نے جامعہ ملیہ میں تعلیم پائی، ان کی وفات سے جامعہ ایک لائق فرزند علمی حلقہ ایک شریف اہل علم اور ملک ایک بہت ہی باوقار محب وطن سے محروم ہوگیا، اﷲ تبارک و تعالیٰ ان کو غریق رحمت کرے، آمین۔ (صباح الدین عبدالرحمن، مارچ ۱۹۷۶ء)
The study examines the impact of climate change on the spread of
some diseases in Thi- Qar Province through collecting and analyzing data
about various weather elements and phenomena of some monitoring
stations ( Nasiriyah ) for a high-temperature climatic cycle of 78 years
(1941-2018). It is divided into seven consecutive and different time
periods, 1941-1951, 1952-1962, and 1963-1973, 1974-1984, 1985-1995,
1996-2006, 2007-2018. These elements and phenomena are solar
radiation, temperatures (maximum and minimum), wind (Dust storm,
rising dust, suspended dust), and the thermal extremes phenomenon (heat
and cold waves) The research aims to reveal the reality of trends in
climate of the province of thi qar, and find out the reality of the general
trend of the elements of climatic different by relying on a series of
evidence statistical number of climatic variables for the meteorological
station in Nasiriyah especially temperature, wind speed, relative humidity
and rainfall, and extreme dust The most important results of the research
showed that temperatures trending upward in sync with a clear reduction
in the amount of relative humidity and rainfall which threatens a sharp
repeating the phenomenon of drought in the future. The research study
has found that the City of Nasiriyah ranked first in human diseases for the
period 2009-2018, as the reasons for this level of diseases include that
Nasiriyah is subject to the recurrence of dusty weather phenomena due to
its proximity to the Western Desert Plateau, as well as the lack of cultivated and water-covered areas. This city witnesses serious air
pollutions due to the concentration of a large number of factories located
near inhabited areas, as well as, the spread of brick factories in the
regions of the city, such as, brick factories in the area of El-Islah. This is
public services, in addition to the building projects, deterioration of
sewage overflow, the spread of epidemics and insects harmful to human
health, other climatic environmental pollutants, such as the spread of
pollen, plant scents and air allergens, which contributed to the increase in
the severity of skin diseases, climate eyes, arthritis and respiratory
allergies. The city of Al-Shatra ranked second in the number of people
with climatic diseases, Al-Rifai ranked third with infected cases, Souk
Al-Shuyoukh ranked fourth, and finally Al-Jibayish ranked fifth and last
in people with climatic human diseases for the period 2009-2018 in Dhi-
qar province due to the same geographical, climatic, medical, and
environmental causes indicated earlier.
Pectinase is a heterogeneous group of enzymes that catalyze the hydrolysis of pectin substances and widely used in food and textile industries. In current study, several bacterial strains were isolated from soil and rotten vegetables and screened for pectinase production. The strain that produced maximum pectinase was identified Bacillus licheniformis based on molecular typing technique using 16S rDNA sequence analysis. B. licheniformis KIBGE-IB21 produced maximum pectinase at 37°C after 48 hours of fermentation. Among various carbon sources, apple pectin (1.0 %) showed maximum enzyme production. Different agro industrial wastes were also used as substrate in batch fermentation and it was found that wheat bran is capable of producing high yield of enzyme. Maximum pectinase production was obtained using yeast extract (0.3 %) as a nitrogen source. The crude pectinase from B. licheniformis KIBGE-IB21 was partially purified using 50 % ammonium sulphate saturation. The partially purified pectinase was characterized with respect to its kinetic properties. Denaturation electrophoresis (SDS PAGE) and in-situ electrophoresis were used to estimate the approximate molecular mass of pectinase from B. licheniformis KIBGE-IB21. Approximate molecular mass was found to be 153,000 daltons. The pectinase showed maximum enzymatic activity at pH-10, 45°C of incubation temperature and 5.0 minutes of reaction time. The enzyme was found to be stable at broad range of pH (frompH-8.0 to pH-10) and retained 100 % of its initial activity after 1 hour. The effect of different metallic cations was tested on pectinase activity and it was observed that all metallic cation showed some inhibitory effect on pectinase activity to some extent except Zn2+ which didn’t show any effect on pectinase activity. Among surface-active detergents, the Tween-80 and Triton X-100 stimulated the 3 pectinase activity up to 7.0 % and 11 %, respectively, whereas SDS inhibited 12 % activity of pectinase. The pectinase showed excellent storage stability at 4 °C and -20°C and showed 95 % and 100 % relative activitiy after 30 days, respectively. For enhancing the operational stability and continuous reusability of enzyme, the partially purified pectinase from B. licheniformis KIBGE-IB21 was immobilized within different polymers including calcium alginate beads, polyacrylamide gel and agar-agar matrix. Among these polymers, polyacrylamide gel was found to be most promising and gave 89 % immobilization yield, followed by agar-agar that retained 80 % activity after immobilization. While less immobilization yield was observed in case of calcium alginate beads that only retained 46 % activity. The reaction time of pectinase for maximum pectinolytic activity was increased from 5.0 to 10 minutes after immobilization. The optimum reaction temperature for maximum enzyme activity was increased from 45 °C to 50 °C and 55 °C when the pectinase was immobilized within agar-agar and calcium alginate beads, respectively, whereas the optimum temperature of pectinase remained same after immobilization within polyacrylamide gel. The optimum pH of pectinase didn’t alter when it was immobilized within polyacrylamide gel and calcium alginate beads. But in case of immobilization of pectinase within agar-agar, the optimum pH was changed from 10 to 9.0 as compared to soluble enzyme. Thermal stability of pectinase was improved after immobilization and immobilized pectinase showed higher toleration against different temperatures as compared to free enzyme. It can be concluded that the entrapment is a simple, single step and promising procedure to immobilized pectinase within different synthetic and non-synthetic polymers and enhanced its catalytic properties.