Abstract: Background and Objective: Carbohydrate Binding Module (CBMs), a non catalytic carbohydrate binding modules present in glycosyl hydrolases, are playing substantial role in localizing the enzyme to the target substrate, disrupting the structure of robust polymers and their presence in pectate lyase is rare. Deduced gene sequence of pectate lyase 1B (pelB) from Bacillus licheniformis (Bli PelB) shows unique structural features containing N-terminal signal peptide following with ricin super family CBM13 and C-terminal catalytic domain. The objective of the study was to characterize Bli PelB and evaluation of role of CBN13 present in Bli PelB sequence. Methodology: Full length and catalytic domain part of pelB was cloned and expressed. Protein was purified through Ni-NTA his tag affinity chromatography and characterized. Results: Biochemical characterization of Bli PelB revealed maximal activity at 50°C with pH 8.0. Enzyme retained more than 80% activity between pH 7.5-9.0. Bli PelB found to be thermostable at 50°C by maintaining more than 60% activity for 4 days. Bli PelB was 100% active on methylated (70-75%) apple pectin as compared to non methylated polygalacturonic acid (PGA) with which it was 29%. Specific activity was found to be 1451±2.0 and 423±3.5 U mg–1 for methylated pectin and PGA, respectively. kcat and kcat/Km is markedly higher for methylated pectin than PGA. In comparison with Bli PelB, C-terminal catalytic domain of Bli PelB (CD Bli PelB) showed 60% decrease in specific activity while 70% decrease in thermal stability and kinetic efficiency. Conclusion: The characterized properties of Bli PelB are suitable for its industrial applications. The reduction in catalytic activity and thermal stability of Bli PelB without CBM13 could explain the role of CBM in enzyme efficiency.