Before the creation of Pākistān, there were multiple points functional as circles of Qur’ānic Durūs. Among these, Dars-e- Qur’ān by Sheikh al Tafsīr Maulānā Aḥmad ‘Alī Lāhorī (d:1381A.H/1962A.D) was of a distinguished standing. Scholars from remote areas of Delhī, Luckhnow, and even of Deobund used to come over here for the genesis of the Qur’ān. Among these personalities is Maulānā Akhlāq Ḥusain Qāsmī of Delhī as well as the famous and great literary figure of the Islamic World Maulānā Abu’l-Ḥasan ‘Alī Nadvī (d:1420A.H/1999A.D). Maulānā ‘Alī Mian made a mention of it in the session of ‘Ālmī Rābitah al Adab al Islāmī in 1999 A.D at Lāhore. He said,“I confess with pride that I have gained a lot from Maulānā Aḥmad ‘Alī Lāhorī”. Moreover, these were not only the orthodox scholars who benefited from Ḥaḍrat Lāhorī but a large number of modern scholars were also on his panel as well-wishers. The name of the famous literary and scholarly figure Dr. Syed ‘Abdallāh (d:1406-A.H/1986A.D) may be quoted as an example. Prior to and after the creation of Pākistān, out of many distinguished Qur’ānic Circles, a few of these are particularly worth mentioning:
Maulānā Abu’l-Ḥasanāt Qādrī (Masjid-e-Wazīr Khān)
Maulānā Dāwūd Ghaznavī (Chuniān Wālī Masjid)
Maulānā Ghulām Murshid (Bādshāhī Masjid)
Maulānā ‘Abdallāh Farūqī (Delhi Muslim Hotel, Old Anār Kalī)
Maulānā Maudūdī (‘Abd al-Karīm Road, Qil‘ah Gojar Singh).
Dr. Isrār Aḥmad was also one of the links in the chain; he established Circles of Durūs-e- Qur’ān not only in Lāhore but in the entire country and invested all his potential to make the message of the Qur’ān so public. This book highlights his services and thoughts. There are five chapters in the book. The first chapter is entitled “Dr. Isrār...
Background and Aim: Social discrimination is one of the most fatal and important source of hindrance for women causing them depressed. The aim of this research study was to find important information on QOL of physically disabled women of backward areas (Triple discriminated population of Pakistan).
Methodology: The current research was conducted at PRSP, D.I.Khan through Cross sectional survey. Sample size for current study was 300 and SF-36 was used to measure QOL. Data was analyzed by using SPSS 22.
Results: The measured mean age of the sample was 27.07 ± 11.10 years. Only 22% of the participants were married. Only 10 3.3% of the participants, completed their tertiary education. The overall SF-36 score was 47.07 ± 12.78. the domains like Physical functioning was 41.33 ± 20.38, Role physical 31.66 ± 35.61, Body pain 74.77 ± 24.06, General health 44.91 ± 14.12, Energy/fatigue 43.16 ± 16.01, Social functioning 49.37 ± 19.80, Role emotional 30.77 ± 36.53, and Mental health 45.97 ± 13.71. This study shows that education has significant impact on the QOL.
Conclusion: Physical disability has visible effects on quality of life of Female PWDs. In PWDs management, quality of life needs to be focused in Rehab program for more effective approach.
Xylanases degrade the hemicellulosic component of plant biomass and find potential applications in poultry, paper, textile and biofuel industries. In this study, a novel, family GH10 enzyme, Xyn10B.CB3B2 from Acidothermus cellulolyticus 11B was characterized. This enzyme was found to be a trifunctional enzyme having endo xylanase, arabinofuranosidase and acetyl xylan esterase activities. Native xylanase, Xyn10B.CB3B2 had carbohydrate binding modules (CBM), CBM3 and CBM2 in tandem at the C-terminus. CBMs are protein domains that bind carbohydrate ligands and are found in carbohydrate active enzymes. Truncation of CBM2 was done to create Xyn10B.CB3 while CBM3 was fused to N-terminus of catalytic domain to form Xyn10B.B3C. Fusion of CBM2 at the C- and N-termini of the catalytic domain resulted in Xyn10B.CB2 and Xyn10B.B2C, respectively. In addition, only the catalytic domain (Xyn10B.C) was also characterized in this study. All of the enzyme variants were successfully expressed in soluble fraction of Escherichia coli cells and purified through binding with regenerated amorphous cellulose except Xyn10B.C that was obtained as inclusion bodies and purified by refolding. Activities of Xyn10B.CB3B2, Xyn10B.CB3, Xyn10B.B3C, Xyn10B.CB2, Xyn10B.B2C and Xyn10B.C on beechwood xylan were 118,305, 68,325, 65,825, 49,261, 44,518 and 40,368 U/μmol, respectively. Activities of Xyn10B.CB3B2, Xyn10B.CB3, Xyn10B.B3C, Xyn10B.CB2, Xyn10B.B2C and Xyn10B.C towards p nitorphenylarabinofuranoside were 9,042, 4,532, 4,026, 5,672, 5,137 and 4,340 U/μmol, respectively. Activities of Xyn10B.CB3B2, Xyn10B.CB3, Xyn10B.B3C, Xyn10B.CB2, Xyn10B.B2C and Xyn10B.C towards p-nitrophenylacetate were 15,545, 10,485, 8,856, 7,820, 7,571 and 7,342 U/μmol, respectively. All of the enzyme variants had optimum temperature 70 °C and optimum pH 6.0, under the vii assay conditions used. However, Xyn10B.C had optimum temperature and pH of 60 °C and 5.0-6.0, respectively. Binding assays revealed that all of the variants bound to insoluble oat spelt xylan and Avicel expect Xyn10B.C that did not bind to Avicel. Incubation of all enzyme variants with Mn2+ had negative impact on the activity of enzymes while other metal ions had no effect on the activity. Xyn10B.CB3B2 was stable up to 70 °C while Xyn10B.CB3, Xyn10B.B3C, Xyn10B.CB2 and Xyn10B.B2C were stable up to 60 °C. Xyn10B.C was stable only up to 50 °C as thermal unfolding was observed beyond these temperatures during CD spectroscopy analysis. All of the enzyme variants were highly active producing xylobiose and xylose as end products, as well as debranching the substrates by removing arabinose and acetyl side chains as observed by HPLC analysis of the lysates and arabinose/acetate assays. This study successfully elucidated the characteristcs of a novel trifunctional xylanase, Xyn10B. Due to its specific characteristics, Xyn10B.CB3B2 and its variants seem to be of importance for industrial applications. In another study, XynI from Caldicellulosiruptor saccharolyticus DSM 8903 was expressed in E. coli as 35.8 kDa protein in soluble form, but the expression level was rather low. MFOLD analysis of the sequence between the ribosomal binding site and the 5¢-end codons of the gene showed that the start codon AUG was trapped in the mRNA secondary structure. Cloning the gene using pET28a(+) increased expression to a level of 35% as compared to about 4% when expressed using pET22b(+). pET28a(+), having His-tag before the start codon, would prevent strong secondary structure formation thus allowing higher expression level. Activity of XynI was found to be 10, 5 and 6 U/mg on beechwood, birchwood and oat spelt xylan, respectively. Further studies are required to elucidate the reasons behind low activity through molecular modelling and docking analyses.