Chymotrypsin from the hepatopancreas of cuttlefish (Sepia officinalis) with high activity in the hydrolysis of long chain peptide substrates: Purification and biochemical characterisation

► Purification of a chymotrypsin from the hepatopancreas of cuttlefish (Sepia officinalis). ► The molecular weight of the purified chymotrypsin was estimated to be 28 kDa by SDS-PAGE. ► The optimum pH and temperature for chymotrypsin activity were around 8.5 and 55 °C, respectively. ► The enzyme was extremely stable in the pH range of 7.0-10.0 and highly stable up to 50 °C after 1 h incubation. ► The N-terminal amino acid sequence of the first 20 amino acids of the purified chymotrypsin was IVGGQEATIGEYPWQAALQV.