Anticoagulant activity of partially purified chitinase produced by Citrobacter freundii str. nov. haritD11 by fermentation of wheat bran coupled with fish scales

Solid phase fermentation of wheat bran coupled with powdered fish scales could yield chitinase using a novel Citrobacter strain. The fermentation conditions are optimized conventionally (84.14 U/gds) and statistically (94.3 U/gds). The partially purified chitinase had a specific activity of 53.41 U/mg with optimal activity at pH 8.5 and 50 °C, it was stable at 7.5–10 pH range for 24 h with more than 80% stability at 45–60 °C, and the Km value of chitinase with swollen chitin (substrate) is 8.11 mg/ml with a V max of 2.43 mmol h −1 ml −1 . The partially purified enzyme was halotolerant showing maximum activity and stability up to 10% of Nacl, also possessing potential anticoagulant activity. This is the first report to date elucidating the production of halotolerant chitinase from wheat bran supplemented with fish scales using Citrobacter freundii haritD11 and its application as an anticoagulant agent and notable tolerance to heavy metal ions.