Chitin and chitinases (EC 3.2.1.14) have an immense potential. Chitinolytic enzymes have wide-ranging applications such as preparation of pharmaceutically important chitooligosaccharides and N-acetyl D-glucosamine, preparation of single-cell protein, isolation of protoplasts from fungi and yeast, control of pathogenic fungi, treatment of chitinous waste, and control of malaria transmission. In this review, we discuss the occurrence and structure of chitin, the types and sources of chitinases, their mode of action, chitinase production, as well as molecular cloning and protein engineering of chitinases and their biotechnological applications.

Biotechnological aspects of chitinolytic enzymes: a review

Chitin is the second most abundant organic and renewable source in nature, after cellulose. Chitinases are chitin-degrading enzymes. Chitinases have important biophysiological functions and immense potential applications. In recent years, researches on fungal chitinases have made fast progress, especially in molecular levels. Therefore, the present review will focus on recent advances of fungal chitinases, containing their nomenclature and assays, purification and characterization, molecular cloning and expression, family and structure, regulation, and function and application.

Review of fungal chitinases.

Chitin is produced in enormous quantities in the biosphere, chiefly as the major structural component of most fungi and invertebrates. Its degradation is chiefly by bacteria and fungi, by chitinolysis via chitinases, but also via deacetylation to chitosan, which is hydrolysed by chitosanases. Chitinases and chitosanases have a range of roles in the organisms producing them: autolytic, morphogenetic or nutritional. There are increasing examples of their roles in pathogenesis and symbiosis. A range of chitinase genes have been cloned, and the potential use for genetically manipulated organisms over-producing chitinases is being investigated. Chitinases also have a range of uses in processing chitinous material and producing defined oligosaccharides.

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Physiology of microbial degradation of chitin and chitosan

https://cyberleninka.org/article/n/328796.pdf

Isolation of novel chitinolytic bacteria and production optimization of extracellular chitinase

Thirteen different chitin-degrading bacteria were isolated from soil and sediment samples. Five of these strains (SGE2, SGE4, SSL3, MG1, and MG3) exhibited antifungal activity against phytopathogenic fungi. Analyses of the 16S rRNA genes and the substrate spectra revealed that the isolates belong to the genera Bacillus or Streptomyces. The closest relatives were Bacillus chitinolyticus (SGE2, SGE4, and SSL3), B. ehimensis (MG1), and Streptomyces griseus (MG3). The chitinases present in the culture supernatants of the five isolates revealed optimal activity between 45°C and 50°C and at pH values of 4 (SSL3), 5 (SGE2 and MG1), 6 (SGE4), and 5–7 (MG3). The crude chitinase preparations of all five strains possessed antifungal activity. The chitinase of MG3 (ChiIS) was studied further, since the crude enzyme conferred strong growth suppression of all fungi tested and was very active over the entire pH range tested. The chiIS gene was cloned and the gene product was purified. The deduced protein consisted of 303 amino acids with a predicted molecular mass of 31,836 Da. Sequence analysis revealed that ChiIS of MG3 is similar to chitinases of Streptomyces species, which belong to family 19 of glycosyl hydrolases. Purified ChiIS showed remarkable antifungal activity and stability.

Enrichment of chitinolytic microorganisms: isolation and characterization of a chitinase exhibiting antifungal activity against phytopathogenic fungi from a novel Streptomyces strain.

J. Lin

Papers

Screening microorganisms for chitin hydrolysis and production of ethanol from amino sugars