قدیم سودی مالیاتی نظام کا تحقیقی جائزہ

Ontemporary modern interest-bearing financial system, “economicsystem”, has become an integral part and the prevalent system reflects that in the modern progressive era of growth where other arts have seen progress than in the old days the modern interest bearing system has become a part of the financial development. Interest in the present era has being understood as a direction for financial growth and development of economy hence in some way or the other been tried to be enforced in to the Islamic world such that it becomes a need and no country can live without. And the objectives of this interest bearing system can meet their targets. In Muslim countries minds that do not have deep commitment with Islamic teaching have been convinced in a way that in the ancient days this level of interest was not needed as in the present era. So, on the interest of present day “riba” can’t be applied whose prohibition is proved by Islamic law. The impression that interest is the need of modern times in ancient times to modern times thislevel of interest is not required, nor was there any specifically organized circle like today concept the financial system may be of interest not only if favor of contemporary practice in the present, but also an extremely ancient system was out there and have some evidence of old banking practices. This article, with the vividness of ancient religions, has proved that “interest” in antiquity is as same as of today. The form of interest and its impacts aren’t get changed by the change in ancient or current business practices. Interest is interest, whether it is found in ancient religions or at theadvent of Islam or even after that in the modern day. It embodies the same “riba” whose prohibition is proved in the Islamic sharia.

Immobilization and Characterization of Pectinase from Bacillus Species Using Different Supports

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.