Chitinases: in agriculture and human healthcare

Nagpure, Anand; Choudhary, Bharti; Gupta, Rajinder K.

doi:10.3109/07388551.2013.790874

Cited by 110 publications

(60 citation statements)

References 242 publications

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“…5) on the catalytic and chitin binding domains of HCHT. The results showed that GH18-containing genes are found in genomes of all domains of life and that this ancestral family of catalytic domains is present in numerous modular enzymes involved in various biological processes 20, 31–33 . It is therefore not surprising that they are associated to a wide variety of domains as it is illustrated by the 377 different architectures classified in Pfam database (http://pfam.xfam.org).…”

Section: Discussionmentioning

confidence: 99%

Human Chitotriosidase: Catalytic Domain or Carbohydrate Binding Module, Who’s Leading HCHT’s Biological Function

Crasson

Courtade

Léonard

et al. 2017

Sci Rep

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Chitin is an important structural component of numerous fungal pathogens and parasitic nematodes. The human macrophage chitotriosidase (HCHT) is a chitinase that hydrolyses glycosidic bonds between the N-acetyl-D-glucosamine units of this biopolymer. HCHT belongs to the Glycoside Hydrolase (GH) superfamily and contains a well-characterized catalytic domain appended to a chitin-binding domain (ChBDCHIT1). Although its precise biological function remains unclear, HCHT has been described to be involved in innate immunity. In this study, the molecular basis for interaction with insoluble chitin as well as with soluble chito-oligosaccharides has been determined. The results suggest a new mechanism as a common binding mode for many Carbohydrate Binding Modules (CBMs). Furthermore, using a phylogenetic approach, we have analysed the modularity of HCHT and investigated the evolutionary paths of its catalytic and chitin binding domains. The phylogenetic analyses indicate that the ChBDCHIT1 domain dictates the biological function of HCHT and not its appended catalytic domain. This observation may also be a general feature of GHs. Altogether, our data have led us to postulate and discuss that HCHT acts as an immune catalyser.

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Section: Discussionmentioning

confidence: 99%

Human Chitotriosidase: Catalytic Domain or Carbohydrate Binding Module, Who’s Leading HCHT’s Biological Function

Crasson

Courtade

Léonard

et al. 2017

Sci Rep

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“…Recently, Streptomyces sp. (Gram-positive, filamentous bacteria) has attracted more attention among researchers because of their ability to suppress growth of a wide variety of phytopathogenic fungi [12,[35][36][37].…”

Section: Discussionmentioning

confidence: 99%

Fungal cell-wall lytic enzymes, antifungal metabolite(s) production, and characterization fromStreptomyces exfoliatusMT9 for controlling fruit-rotting fungi

Choudhary

Nagpure

Gupta

2014

J. Basic Microbiol.

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An antifungal actinomycete strain MT9 was isolated from Loktak Lake, Manipur, India and its cultural characteristics, fatty acid methyl ester, 16S rRNA gene analysis suggests that strain MT9 is identical to Streptomyces exfoliatus. Strain MT9 displayed strong and broad-spectrum antagonism towards several fruit-rotting fungi by mycelial growth suppression. Crude fungal cell-wall lytic enzymes, i.e., chitinase, β-1,3-glucanase, and protease produced by S. exfoliatus MT9 were optimally active at pH 8.0 and 50 °C, pH 5.0 and 60 °C, pH 9.0 and 70 °C, respectively. All three mycolytic enzymes had good stability over a wide pH range of 5.0-10.0, with protease being more thermostable than both chitinase and β-1,3-glucanase. Interestingly zymogram analysis revealed that S. exfoliatus MT9 secretes six distinct chitinase isoenzymes with approximate molecular weights of 9.42, 13.93, 27.87, 36.43, 54.95, 103.27 kDa, six active protease isoenzymes with apparent molecular weights of 12.45, 30.20, 37.45, 46.32, 52.46, 131.46 kDa, and an active band of 119.39 kDa as β-1,3-glucanase enzyme. Extracellular fluid and its organic solvent extracts also exhibited inhibitory activity to various fruit-rotting fungi. The MIC value of n-butanol extract was 2-25 µg/ml against tested fruit-rotting fungi. Antifungal secondary metabolite(s) was found to be polyene in nature. To the best of our knowledge, this is the first report on extracellular production of fungal cell-wall lytic enzymes and antifungal metabolites by bioactive S. exfoliatus MT9 under submerged fermentation.

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“…Endokitinase memotong polimer kitin secara acak dan menghasilkan dimer, trimer, tetramer, dan oligomer gula. N-asetil-glukosaminidase yang memutuskan diasetilkitobiosa dan menghasilkan NAG (Dahiya et al, 2006;Herdyastuti et al, 2009 (Nagpure et al, 2014).…”

Section: Screening and Chitinolytic Activity Evaluation Of Nine Indigunclassified

Skrining dan Evaluasi Aktivitas Kitinase dari Sembilan Isolat Bakteri Lokal

Maggadani¹,

Setyahadi²,

Harmita³

2017

Pharm Sci Res

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AbstrakKitinase merupakan enzim yang mendegradasi kitin pada ikatan β-1,4-asetamido-2-deoksi-D-glikosida menjadi produk turunannya yaitu kitin oligosakarida atau monomer N-asetilglukosamin (NAG). Enzim kitinase dihasilkan oleh mikroorganisme kitinolitik yang sebagian besar terdapat di lingkungan tanah dan air. Kitinase dimanfaatkan pada bidang pertanian sebagai agen biokontrol. Produk hasil hidrolisisnya dimanfaatkan dalam bidang kesehatan dan kosmetik sebagai suplemen anti inflamasi dan anti hiperpigmentasi. Penelitian kali ini bertujuan untuk skrining dan evaluasi kemampuan 9 bakteri isolat dalam menghasilkan kitinase. Isolat yang terbaik adalah isolat yang menghasilkan kitinase dengan aktivitas yang tinggi dan mampu menghidrolisis kitin menjadi monomer NAG. Dari 9 isolat bakteri tersebut, bakteri BPPTCC-2 merupakan bakteri yang terpilih karena mampu menghasilkan kitinase dengan aktivitas tertinggi yaitu 0,1780 U/mL. Kitinase tersebut dapat menghidrolisis substrat kitin dan menghasilkan NAG sebagai produk tunggal dan dengan rendemen NAG paling tinggi yaitu 11,5%. AbstractChitinase is an enzyme that degrades chitin on β-1,4-acetamido-2-deoxy-D-glycoside bound to produce Chitin oligosaccharide or its soluble monomer, N-acetylglucosamine (NAG). Chitinase are usually produced naturally by chitinolytic microorganism that are found in soil or water environment. Chitinase have been widely used for biocontrol agents of plant pests. The product from chitinase hydrolysis can be used as antiinflammatory agent and anti hyperpigmentation. This research was aimed to screen and evaluate the chitinolytic ability of 9 isolate. The best isolate was the one which produced high chitinolytic activity and hydrolyzed chitin into NAG. 9 isolate were examined and BPPTCC-2 was the best isolate which produced highest level of chitinolytic activity 0.1780 U/ml. The chitinase was able to hydrolyzed chitin resulting high yields of NAG 11.5% as the only product.

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Chitinases: in agriculture and human healthcare

Cited by 110 publications

References 242 publications

Human Chitotriosidase: Catalytic Domain or Carbohydrate Binding Module, Who’s Leading HCHT’s Biological Function

Human Chitotriosidase: Catalytic Domain or Carbohydrate Binding Module, Who’s Leading HCHT’s Biological Function

Fungal cell-wall lytic enzymes, antifungal metabolite(s) production, and characterization fromStreptomyces exfoliatusMT9 for controlling fruit-rotting fungi

Skrining dan Evaluasi Aktivitas Kitinase dari Sembilan Isolat Bakteri Lokal

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