Accéder au contenu
Merck

C6137

Chitinase from Streptomyces griseus

lyophilized powder (essentially salt free), ≥200 units/g solid

Synonyme(s) :

N-acetyl-glucosaminidasechitobiase, Chitin digestion enzymes, poly(β-(1→4)-[2-acetamido-2-deoxy-D-glucoside])- glycanohydrolase

Se connecter pour consulter les tarifs organisationnels et contractuels.

Sélectionner une taille de conditionnement

Changer de vue

A propos de cet article

UNSPSC Code:
12352204
EC Number:
232-578-7
NACRES:
NA.54
Specific activity:
≥200 units/g solid
Service technique
Besoin d'aide ? Notre équipe de scientifiques expérimentés est là pour vous.
Laissez-nous vous aider


form

lyophilized powder (essentially salt free)

Quality Segment

specific activity

≥200 units/g solid

mol wt

30 kDa

solubility

H2O: soluble 0.90-1.10 mg/mL

storage temp.

−20°C

General description

Chitinase is an extracellular complex of enzymes that degrade chitin. Chitin is a cell wall component of Fungi and exoskeketal essentials of different organisms which reshape their own chitin or digest/dissolve the chitin of other organisms (insects, fungi, yeast, and algae, and in the internal structures of other vertebrates) . Chitinases have been detected in many microorganisms and in plants. In fungi, chitinases assist in morphogenesis, to break down the inherent chitin content of fungal cell walls. Plant chitinases help in resistance to fungal attack and counteracting fungal growth, by targeting those same fungal cell walls. In bacteria, bacterial chitinases assist in utilizing chitin as a carbon source and as an energy source.Streptomyces griseus produces multiple chitinases of different molecular masses after growth induction with chitin as the carbon source.

The enzymatic hydrolysis of chitin to N-acetyl-D-glucosamine involves two consecutive enzyme reactions:
  • The first reaction, chitodextrinase-chitinase, is a poly(β-(1→4)-[2-acetamido-2-deoxy-D-glucoside])- glycanohydrolase, which removes chitobiose units from chitin.
  • The second activity is N-acetyl-glucosaminidasechitobiase, which cleaves the disaccharide to its monomer subunits, N-acetyl-D-glucosamine.

Application

Agriculture fields: control pathogens.
Human health care: Asthma.
Pharma: preparation of 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

Biochem/physiol Actions

Chitinase is an extracellular enzyme complex that degrades chitin and has a molecular mass of approximately 30 kDa. Chitin is degraded to N-acetyl-D-glucosamine in 2 enzymatic reactions. Firstly, chitobiose units are removed from chitin by chitodextrinase-chitinase. The second reaction involves N-acetyl-glucosaminidase-chitobiase, which cleaves the disaccharide to its monomer subunits (that comprise of N-acetyl-D-glucosamine). The optimum reaction temperature is 37 °C.

Features and Benefits

Chitinase is an extracellular complex of enzymes that degrade chitin. It is a lytic enzyme suitable for fungal cell walls lysis.

Other Notes

One unit will liberate 1.0 mg of N-acetyl-D-glucosamine from chitin per hour at pH 6.0 at 25 °C in a 2 hour assay.
One new 1 hour unit = approx. 50 old 48 hour units.


Still not finding the right product?


Pictogrammes

Health hazard

Mot-clé

Danger

Codes de danger

Mentions de précaution

Hazard Classifications

Resp. Sens. 1

Classe de stockage

11 - Combustible Solids

Que se passe-t-il ?

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

EPI (équipement de protection individuelle)

Eyeshields, Gloves, type N95 (US)



Faites votre choix parmi les versions les plus récentes :

Certificats d'analyse (COA)

Lot/Batch Number

Vous ne trouvez pas la bonne version ?

Si vous avez besoin d'une version particulière, vous pouvez rechercher un certificat spécifique par le numéro de lot.

Déjà en possession de ce produit ?

Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents