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C8241

Chitinase from Trichoderma viride

lyophilized powder, ≥600 units/g solid

Synonym(s):

N-acetyl-β-glucosaminidase and chitodextrinase

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25 UNITS

$451.00

$451.00


Available to ship onMarch 18, 2026Details


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About This Item

UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-578-7
MDL number:
EC Number:
Specific activity:
≥600 units/g solid

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form

lyophilized powder

Quality Level

specific activity

≥600 units/g solid

mol wt

30 kDa

solubility

0.05 M phosphate buffer, pH 6.0: soluble 0.90-1.10 mg/mL, faintly hazy to hazy (with particles)

shipped in

wet ice

storage temp.

−20°C

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This Item
C6137SAE0158219466
specific activity

≥600 units/g solid

specific activity

≥200 units/g solid

specific activity

>200 USP units/mg solid

specific activity

≥10,000 units/g dry wt.

form

lyophilized powder

form

lyophilized powder (essentially salt free)

form

-

form

solid

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

2-8°C

mol wt

30 kDa

mol wt

30 kDa

mol wt

-

mol wt

-

shipped in

wet ice

shipped in

-

shipped in

wet ice

shipped in

ambient

solubility

0.05 M phosphate buffer, pH 6.0: soluble 0.90-1.10 mg/mL, faintly hazy to hazy (with particles)

solubility

H2O: soluble 0.90-1.10 mg/mL

solubility

-

solubility

water: soluble

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 a 30 kDa (approx.) extracellular enzyme complex that degrades chitin. Chitin is degraded to N-acetyl-D-glucosamine in 2 enzymatic reactions. Firstly, chitobiose units are removed from chitin by chitodextrinase-chitinase, a poly(1,4-β-[2-acetamido-2-deoxy-D-glucoside])-glycanohydrolase. The second reaction involves N-acetyl-glucosaminidase-chitobiase, which cleaves the disaccharide to its monomer subunits of N-acetyl-D-glucosamine. The enzyme may be classified into endo- and exochitinase. The endochitinase activity involves random cleavage at internal points in the chitin chain. The exochitinase activity consists of a progressive action which starts at the non-reducing end of chitin and releases chitobiose or N-acetyl-glucosamine units.[1] The chitinolytic enzymes from T. viride are a mixture of extracellular chitinolytic enzymes, which exhibit exo- and endochitinase activities. The major activity was found to be that of N-acetyl-β-glucosaminidase.
Chitinase serves as a biopesticide against several fungi and insects. This hydrolytic enzyme is capable of cleaving the glycosidic bonds in chitin.

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.

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Storage Class

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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Marion Schiavone et al.
FEMS yeast research, 14(6), 933-947 (2014-07-22)
A reliable method to determine cell wall polysaccharides composition in yeast is presented, which combines acid and enzymatic hydrolysis. Sulphuric acid treatment is used to determine mannans, whereas specific hydrolytic enzymes are employed in a two sequential steps to quantify
Functional Microbial Diversity: Functional Genomics and Metagenomics Using MAPLE
Microbial Diversity in the Genomic Era, 427-449 (2019)
Antifungal effect and chitinase activities of the froth of spittlebug Poophilus costalis (Walker)(Hemiptera: Cercopoidea: Aphrophoridae)
Chang SC, et al.
Journal of Asia-Pacific Entomology, 22(1), 269-273 (2019)
Chitinases
Enzymes in Human and Animal Nutrition, 361-378 (2018)
Production of microbial chitinases-a revisit.
PA Felse, T Panda
Bioprocess and Biosystems Engineering, 23, 127-134 (2000)

Global Trade Item Number

SKUGTIN
C8241-25UN04061833521953

Questions

  1. Hello, Do you have the information about the activity of te enzyme in different pH values? Chitinase from Trichoderma viride

    1 answer
    1. The activity of this enzyme has not been characterized across the pH range. However, information available in the product data-sheet indicates that the enzyme should be active within mildly acidic to neutral conditions. Please see the link below to review this datasheet:
      https://www.sigmaaldrich.com/deepweb/assets/sigmaaldrich/product/documents/402/519/c8241dat-ms.pdf

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