Isolation, identification and molecular characterization of CelA-BL (Cellobiosidase) gene from Bacillus licheniformis NCIM 5556, isolated from Unhale Hot spring, Rajapur, Ratnagiri, Maharastra, India, using Next generation Sequence technology.

Bacteria are well known to produce cellulase enzymes either single peptide enzymes or multi-enzyme components. Recombinant DNA technology is a well-known tool can facilitate to better understand the regulatory and catalytic activity of the cellulase system. Endo-cellulase and exocellulase are the major enzymes which synergistically act on crystalline cellulose and converts into cellobiose, further converted to simple glucose units with the help of ß-glucosidase. Fungal and bacterial cultures produce extracellular nature of cellulase enzymes in a complexed manner, but few bacteria, Clostridia secrets highly structured cellulose hydrolytic complexes called as cellulosomes. Considerable research works have been done to exploit the current need of cellulase enzyme. Studies of these microbial enzymes give a better understanding about the nature of cellulase production and also their catalytic mechanisms. Moreover, cellulases from thermophiles also provide new insights into the structural variation and its catalytic functions. Cellobiosidase is the important enzyme to break cellulose to simple sugars and the gene was isolated from Bacillus licheniformis NCIM 5556 which was isolated from isolated from Unhale Hot spring, Rajapur, Ratnagiri, Maharastra, India, using Next generation Sequence technology. Amplicon sequencing libraries were prepared with Illumina-compatible NEXTflex DNA Sequencing kit and the sequence was subjected on an Illumina sequencer for 150 bp paired-end chemistry.