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Merck

C6137

Chitinase from Streptomyces griseus

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

동의어(들):

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

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UNSPSC Code:
12352204
EC Number:
232-578-7
NACRES:
NA.54
Specific activity:
≥200 units/g solid
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form

lyophilized powder (essentially salt free)

Quality Level

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.


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pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

저장 등급

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)



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세포 용해 완충액, 단백질 추출 키트, 추출 효소, 기타 단백질 분리 및 정제를 위한 용해 강화제와 같은 세포 용해 및 단백질 추출 시약을 찾아보세요.

Cell lysis and protein extraction methods overview various techniques, from detergent solubilization to mechanical disruption, supporting research needs.

관련 콘텐츠 모두 보기

Maimouna Cissoko et al.
Frontiers in plant science, 9, 1494-1494 (2018-11-09)
Actinorhizal plants are able to establish a symbiotic relationship with Frankia bacteria leading to the formation of root nodules. The symbiotic interaction starts with the exchange of symbiotic signals in the soil between the plant and the bacteria. This molecular
Chitinase-resistant hydrophilic symbiotic factors secreted by Frankia activate both Ca(2+) spiking and NIN gene expression in the actinorhizal plant Casuarina glauca.
Chabaud, et al.
The New phytologist, 209, 86-93 (2020)
S Machida et al.
The Journal of biological chemistry, 268(3), 1702-1707 (1993-01-25)
The membrane-bound chitin synthase, a key enzyme of chitin biosynthesis, was purified, for the first time to homogeneity as a zymogen form. Digitonin could solubilize the enzyme from microsomal fraction of the filamentous fungus Absidia glauca, with 60-70% of the