Abstract
Hagfish belongs to cyclostomata which has different characteristics from teleost and chondrichthyes. So, they are considered to have important taxonomic position. They are consumed as food and their skin can be used for leather. Cathepsin B is an enzyme classified as cysteine protease and papain family. Also, it can act as endopeptidase. It is involved in the process to degrade proteins in lysosome. In this research, we identified nucleotide and amino acid sequence of cathepsin B in Eptatretus burgeri. The nucleotide sequence length of EbCtsB is 1694 bp including 5’-UTR (107 bp), ORF (1002 bp), and 3’-UTR (585 bp). ORF encode 333 AA (amino acid sequences) which molecular weight is 36.8 kDa. And we purified recombinant EbCtsB and conducted activity assay using diverse pH condition, substrates, inhibitors, metal ions, and detergents. Z-RR-AMC considered as good substrate of EbCtsB have optimal activity at pH 7.5. Antipain is the best inhibitor of EbCtsB. Also, ZnSO₄, CuSO₄, and HgCl₂ can decrease the activity of EbCtsB. MgSO₄ and CaCl₂ can increase its activity. In the presence of SDS, the activity of EbCtsB is decreased.
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