Chitinase

Ayokunmi OyeleyeYahaya M.

Molecular and Cellular Pediatrics volume 2 , Article number: 3 Cite this article. Metrics details. Chitin, after cellulose, the second most abundant biopolymer on earth, is a key component of insects, fungi, and house-dust mites. Lower life forms are endowed with chitinases to defend themselves against chitin-bearing pathogens. Unexpectedly, humans were also found to express chitinases as well as chitinase-like proteins that modulate immune responses. Particularly, increased levels of the chitinase-like protein YKL have been associated with severe asthma, cystic fibrosis, and other inflammatory disease conditions. Here, we summarize and discuss the potential role of chitin, chitinases, and chitinase-like proteins in pediatric lung diseases.

Chitinase

Federal government websites often end in. The site is secure. Chitin, the second most abundant polysaccharide in nature after cellulose, is found in the exoskeleton of insects, fungi, yeast, and algae, and in the internal structures of other vertebrates. Chitinases are enzymes that degrade chitin. Chitinases contribute to the generation of carbon and nitrogen in the ecosystem. Chitin and chitinolytic enzymes are gaining importance for their biotechnological applications, especially the chitinases exploited in agriculture fields to control pathogens. Chitinases have a use in human health care, especially in human diseases like asthma. Chitinases have wide-ranging applications including the 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, mosquito control and morphogenesis, etc. In this review, the various types of chitinases and the chitinases found in different organisms such as bacteria, plants, fungi, and mammals are discussed. Chitin and its associated materials have a broad usage in drug delivery, wound healing, dietary fiber, and in waste water treatment. These 2 forms of chitin vary in packing and polarities of adjacent chains in the succeeding sheets. The catabolism of chitin takes place in 2 steps, involving the initial cleavage of the chitin polymer by chitinases into chitin oligosaccharides and further cleavage to N-acetylglucosamine, and monosaccharides by chitobiases. Chitinases E. Chitinases have the ability to degrade chitin directly to low molecular weight chitooligomers, which serve a broad range of industrial, agricultural, and medical functions such as elicitor action and anti-tumor activity. Several pathogens contain chitin coats, giving them protection against both external and internal in a host environment.

Chitinases have the ability to degrade chitin directly to low molecular weight chitooligomers, chitinase, which serve a broad range of industrial, agricultural, and medical functions chitinase as elicitor action and anti-tumor activity.

Federal government websites often end in. The site is secure. Chitin is a polysaccharide that forms the outer layer of many organisms, and it is widely used in industry. Chitinases are enzymes that can break down chitin into monomeric molecules and are used in the agro-industrial sectors. Because chitin is the key structural component of marine mollusks, crustaceans, and marine invertebrates and other species algae, fungi, and insects , chitinases can be employed in the marine waste management and biocontrol of pathogenic fungi and harmful insects. Chitinase also has uses in the food industry, cosmetics, medicine, waste management, crop protection, and the production of single-cell proteins, among others.

Federal government websites often end in. The site is secure. Food allergies originate from adverse immune reactions to some food components. Ingestion of food allergens can cause effects of varying severity, from mild itching to severe anaphylaxis reactions. Currently there are no clues to predict the allergenic potency of a molecule, nor are cures for food allergies available. Cutting-edge research on allergens is aimed at increasing information on their diffusion and understanding structure-allergenicity relationships. In this context, purified recombinant allergens are valuable tools for advances in the diagnostic and immunotherapeutic fields. Chitinases are a group of allergens often found in plant fruits, but also identified in edible insects. They are classified into different families and classes for which structural analyses and identification of epitopes have been only partially carried out. Moreover, also their presence in common allergen databases is not complete.

Chitinase

This article has been reviewed according to Science X's editorial process and policies. Editors have highlighted the following attributes while ensuring the content's credibility:. Pear ring rot, a significant threat to pear production, is caused by Botryosphaeria dothidea, leveraging the complex dynamics of reactive oxygen species ROS during infection. Initially, plants employ their innate immune system, detecting pathogens through conserved molecular patterns and triggering a defense mechanism that includes ROS bursts, restricting pathogen growth. However, B. The current challenge lies in understanding how plants manage ROS levels to maintain resistance against B. In this study, researchers employed comparative transcriptome analysis to delve into the molecular dynamics of pear resistance to Botryosphaeria dothidea infection, pinpointing chitinase PbrChiAas a crucial regulator. By contrasting susceptible and resistant pear cultivars, the research unveiled that PbrChiA not only exhibits direct antifungal activity but also mitigates chitin-induced ROS accumulation by interacting with PbrLYK1b2, thereby enhancing pear's defense mechanisms. The analysis spanned early to later stages of infection , revealing a distinct upregulation of defense-related genes and pathways, such as photosynthesis inhibition and MAPK signaling, in the resistant cultivar, alongside heightened enzyme activities and reduced ROS levels, contributing to its resilience.

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Chitinases find their use in other fields like agriculture and mosquito control. The CID is absent in Sm ChiC suggesting that its catalytic cleft is more open and shallow compared to its counterparts Figure 4 [ 74 ]. Chitinases having a CBD and aromatic residues are reported to be more efficient in degrading crystalline chitin, while those lacking a CBD may prefer less crystalline forms [ 72 , 73 , 80 ]. However, recently their utilization has attracted increased scrutiny since chemical fungicides are highly toxic. Bacteria, fungi, and insect chitinases are the most diverse members of this family. AIMS Microbiol. GH18 is the most studied family of chitinases, even though chitinolytic enzymes come from a variety of glycosyl hydrolase GH families. Cite this article Mack, I. Table 1 is a list of some chitinases with 3D structures. Cloning and characterization of a small family 19 chitinase from moss Bryum coronatum. The molecular weight of chitinases obtained from Enterobacter sp. An endo-cleaving chitodextrinase EC 3. Molecular Biology of the Cell. Purification and characterisation of an acidic and antifungal chitinase produced by a Streptomyces sp.

Federal government websites often end in. The site is secure. Background: Chitinases are the evolutionary conserved glycosidic enzymes that are characterized by their ability to cleave the naturally abundant polysaccharide chitin.

Fu et al. In the apple plant, the PR4 group is responsible for chitin recognition and the resistance response. Class II chitinases did not have the cysteine-rich N -terminal but had a similar sequence to Class I chitinases. Publisher: Portland Press Ltd. Kathleen Van de Velde, K. Chitinases hydrolyze the chitin present in the waste products and release simpler products, which can be further used to grow yeast and other microbes to generate SCP. J Asthma 48 8 —, doi Wang D. DC14, - 65 9. Purification and some properties of six chitinases from Aeromonas sp. Applications of Chitinases Chitinases have a wide array of applications in various fields, including medical, industrial, and agricultural, which are elaborately discussed below. However, one example of a Class V chitinase showed two chitin binding domains in tandem, and based on the gene sequence, the cysteine-rich N -terminal seemed to have been lost during evolution, probably due to less selection pressure that caused the catalytic domain to lose its function.