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.