Purification and properties of plant chitinases: A review

Easier susceptibility of plants toward vulnerable pathogens due to lack of an immune system necessitated evolution of different kind of responses priming the release of pathogenesis-related (PR) defense proteins. With reference to attack of fungal pathogens, the lytic enzyme known as chitinase (EC 3.2.1.14) could easily degrade the fungal cell wall chitin and played a crucial role in defending plants. In the present review, various chitinases purified from different plant sources with elaboration of their properties have been explored in detail. Purification studies of chitinases showed a diverse range of molecular mass (25–40 kDa), optimum pH (4.0–6.0), temperature (50–60°C), and kinetic parameters. Along with this, purified chitinases also showed strong antifungal activity against phytopathogenic fungi and nonpathogenic plant fungi. Practical applications The present review provides a single platform for all the purification protocols adopted for purification of plant chitinases in a single article. It results into simplification of study of plant chitinases purified from different parts of plants so far. For the readers, who want to be benefitted with the summarized study of plant chitinases and their properties, this review article fulfills their need and quite helpful in context of other review article. Along with this, the review emphasizes on the antifungal properties of plant-purified chitinases and seems to be helpful for those who want to employ these chitinases as a biocontrol agent at larger scale in managing plant fungal diseases.