Enhanced biological activity of chitinase immobilized on cobalt metal-organic framework: Isolation, characterization,...

Chitinase, an enzyme that hydrolyzes glycosidic bonds in chitin, holds significant potential for industrial applications, including biological control, antifungal treatments, and antibiofilm strategies. In this study, chitinase derived from Planomicrobium sp. (PP133202) was immobilized onto a cobalt metal-organic framework (Co-MOF), and its properties were extensively analyzed using various biological, chemical, and physical characterization techniques. The microbial source was identified via 16S rRNA sequencing, and enzyme activity was optimized under submerged conditions using Response Surface Methodology (RSM). Structural and morphological characterization of the chitinase/Co-MOF complex was conducted through FTIR, SEM, TEM, XPS, XRD, EDX, and surface area analyses. The encapsulation efficiency and loading capacity were determined to be 42 % and 20 %, respectively. Notably, the immobilized chitinase exhibited a threefold increase in enzymatic activity compared to its free form. Additionally, the chitinase/Co-MOF complex demonstrated enhanced biological control efficacy, effectively inhibiting Tribolium castaneum and multiple pathogenic microorganisms, including Pseudomonas aeruginosa, Aspergillus flavus, Aspergillus terreus, and Beauveria bassiana. These findings highlight the potential of chitinase/Co-MOF as a promising agent for antimicrobial and pest control applications.