Purification and biochemical characterization of chitinase of Aeromonas hydrophila SBK1 biosynthesized using crustacean shell

Abstract Valorization of shrimp shells as the sole C/N source for chitinase biosynthesis by Aeromonas hydrophila SBK1 was carried out in solid state fermentation. Chitinase (58.6 kDa) was purified from the ferments to homogeneity have K m and V max of 5.5 mg/ml and 39.2 µmol/min for colloidal chitin, respectively. The enzyme was found stable in a range of pH (5.0–10.0), high NaCl concentration (5 M) and at 50 °C temperature. It showed optimal activity at pH 7.0 and 40 °C temperature and contains 52.9% α-helix, 21.5% β-pleated sheet and 10.1% turn in this condition. The enzyme is not a metallo-enzyme, inhibited by Hg 2+ , marginally activated by Tween 60, Tween 80 and SDS (at 1% level), and reasonably stable in presence of DMSO, β-mercaptoethanol, PMSF, sodium azide. The stability of the chitinase at varied conditions assures its employment in industrial sectors.