eng Oriental Scientific Publishing Company Biosciences Biotechnology Research Asia 0973-1245 2023-09-30 20 3 897 906 10.13005/bbra/3141 47047 article Vinita Yadav 1 Sadhana Nighojkar 2 School of Biotechnology, Devi Ahilya University Indore (M.P) India Mata Gujri College of Professional Studies, Indore (M.P) India CDH, an enzyme produced by wood-decomposing fungi, has diverse applications in biosensor production, bioremediation, and biomedical industries. In this study, CDH from Schizophyllum commune BCC26414 was purified using ammonium sulfate precipitation, DEAE-cellulose chromatography, and Sephadex G-200 chromatography. The purification fold achieved was 65.81 with a specific activity of 1612.34 U/mg. The purity and molecular weight of CDH was confirmed using native and SDS PAGE. Optimal temperature and pH were found to be 30°C and 5, respectively. The purified CDH exhibited stability over a wide pH range (3.5 to 6.5) for 24 hrs and retained complete activity at 40°C, with reduced activity at 50°C when observed for 150 min. KCl, MgSO₄, ZnSO₄, and NiCl₂ at a concentration of 5 mM enhanced CDH activity and HgCl₂ and CuSO₄ inhibited the enzyme activity. The kinetic constants, K_m and V_max of CDH for lactose were observed to be 125 mM and 13.26 U/ml, respectively. The purified CDH may be utilized commercially in various applications. https://www.biotech-asia.org/vol20no3/cellobiose-dehydrogenase-from-schizophyllum-commune-bcc26414-purification-and-characterization/ DEAE-cellulose anion exchange chromatography; Purification fold; Schizophyllum commune BCC26414; Sephadex G-200 gel filtration chromatography; Specific activity