|PDB structures||RCSB PDB PDBe PDBsum|
|Locus||Chr. 1 p13.1-21.3|
|chitinase 1 (chitotriosidase)|
|Locus||Chr. 1 q31-q32|
Chitinases (EC 18.104.22.168, chitodextrinase, 1,4-beta-poly-N-acetylglucosaminidase, poly-beta-glucosaminidase, beta-1,4-poly-N-acetyl glucosamidinase, poly[1,4-(N-acetyl-beta-D-glucosaminide)] glycanohydrolase, (1->4)-2-acetamido-2-deoxy-beta-D-glucan glycanohydrolase) are hydrolytic enzymes that break down glycosidic bonds in chitin.
As chitin is a component of the cell walls of fungi and exoskeletal elements of some animals (including worms 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 (barley seed chitinase: EC 22.214.171.124); 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.,
Although mammals do not produce chitin, they have two functional chitinases, Chitotriosidase (CHIT1) and acidic mammalian chitinase (AMCase), as well as chitinase-like proteins (such as YKL-40) that have high sequence similarity but lack chitinase activity.
Like cellulose, chitin is an abundant biopolymer that is relatively resistant to degradation. It is typically not digested by animals, though certain fish are able to digest chitin. It is currently assumed that chitin digestion by animals requires bacterial symbionts and lengthy fermentations, similar to cellulase digestion by ruminants. Nevertheless, chitinases have been isolated from the stomachs of certain mammals, including humans. Chitinase activity can also be detected in human blood and possibly cartilage. As in plant chitinases this may be related to pathogen resistance.
Human chitinases may explain the link between some of the most common allergies (dust mites, mold spores—both of which contain chitin) and worm (helminth) infections, as part of one version of the hygiene hypothesis (worms have chitinous mouthparts to hold the intestinal wall). Finally, the link between chitinases and salicylic acid in plants is well established[further explanation needed]—but there is a hypothetical link between salicylic acid and allergies in humans.
Presence in food
Chitinase occurs naturally in many common foods. This is at least one cause of the cross-reaction phenomenon in latex-fruit syndrome. Bananas, chestnuts, kiwis, avocados, papaya, and tomatoes, for example, all contain significant levels of chitinase.
Chitinases has a wealth of applications, some of which has already been realized by the industry. This includes bio-conversion of chitin to useful products such as fertilizer, the production of non-allergenic, non-toxic, biocompatible, and biodegradable materials (contact lenses, artificial skin and stitches with these qualities are already being produced) and enhancement of insecticides and fungicides.
Possible future applications of chitinases are as food additives to increase shelf life, therapeutic agent for asthma and chronic rhinosinusitis, as an anti-fungal remedy, an anti-tumor drug and as a general ingredient to be used in protein engineering.
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- Chitinase at the US National Library of Medicine Medical Subject Headings (MeSH)
- The X-ray structure of a chitinase from the pathogenic fungus Coccidioides immitis