Chitinases (, chitodextrinase, 1,4-β-poly-N-acetylglucosaminidase, poly-β-glucosaminidase, β-1,4-poly-N-acetyl glucosamidinase, poly[1,4-(N-acetyl-β-D-glucosaminide)] glycanohydrolase, (1→4)-2-acetamido-2-deoxy-β-D-glucan glycanohydrolase; systematic name (1→4)-2-acetamido-2-deoxy-β-D-glucan glycanohydrolase) are hydrolytic enzymes that break down glycosidic bonds in chitin. They catalyse the following reaction: Random endo-hydrolysis of N-acetyl-β-D-glucosaminide (1→4)-β-linkages in chitin and chitodextrins As chitin is a component of the cell walls of fungi and exoskeletal elements of some animals (including mollusks and arthropods), chitinases are generally found in organisms that either need to reshape their own chitin or dissolve and digest the chitin of fungi or animals. Chitinivorous organisms include many bacteria (Aeromonads, Bacillus, Vibrio, among others), which may be pathogenic or detritivorous. They attack living arthropods, zooplankton or fungi or they may degrade the remains of these organisms. Fungi, such as Coccidioides immitis, also possess degradative chitinases related to their role as detritivores and also to their potential as arthropod pathogens. Chitinases are also present in plants – for example barley seed chitinase: , . Barley seeds are found to produce clone 10 in Ignatius et al 1994(a). They find clone 10, a Class I chitinase, in the seed aleurone during development. Leaves produce several isozymes (as well as several of β-1,3-glucanase). Ignatius et al 1994(b) find these in the leaves, induced by powdery mildew. Ignatius et al also find these (seed and leaf isozymes) to differ from each other. Some of these are pathogenesis related (PR) proteins that are induced as part of systemic acquired resistance. Expression is mediated by the NPR1 gene and the salicylic acid pathway, both involved in resistance to fungal and insect attack. Other plant chitinases may be required for creating fungal symbioses.

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