Chitinases are hydrolytic enzymes that play a crucial role in the degradation of chitin, a major component of arthropod exoskeletons and fungal cell walls. This study focused on the isolation, purification and characterization of chitinase from Pseudomonas protegens strain CRML-4. The enzyme was produced using solid-state fermentation with colloidal chitin as an inducer. Crude chitinase was extracted and stepwise ammonium sulfate precipitation (20–80% saturation) revealed maximum protein content and chitinolytic activity in the 20% fraction. Further purification was achieved by gel filtration chromatography on a Sephadex G-100 column, with active fractions identified by co-elution of protein (A280) and enzymatic activity. The purified enzyme’s homogeneity was confirmed through reverse phase high performance liquid chromatography (RP-HPLC) and SDS-PAGE which indicated a single protein band of approximately 55 kDa. Peptide mass fingerprinting via MALDI-TOF-MS identified the enzyme as chitinase C, closely related to Pseudomonas aeruginosa with a 95% identity score. In silico characterization revealed the enzyme to be a stable, acidic protein (pI 5.22) with an aliphatic index of 81.04 and a predominance of random coil structures. Three-dimensional modelling supported by I-TASSER and Ramachandran plot validation confirmed structural reliability and gene ontology analysis linked the enzyme to extracellular chitin catabolic processes. These findings demonstrate that the chitinase from P. protegens CRML-4 is a homogeneous, stable enzyme with promising biotechnological and industrial applications in chitin bioconversion and biocontrol.