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SAE0158

Sigma-Aldrich

Chitinase from Streptomyces griseus

chromatographically purified, lyophilized powder, free of DNA contaminants, suitable for Microbiome research

Synonym(s):

Chitinase from Streptomyces griseus, (1→4)-2-acetamido-2-deoxy-beta-D-glucan glycanohydrolase), Chitodextrinase, Hydrolitic enzyme, Lytic Enzyme, Poly(β-(1→4)-[2-acetamido-2-deoxy-D-glucoside]) glycanohydrolase, Poly(1,4-β-[2-acetamido-2-deoxy-D-glucoside]) glycanohydrolase, beta-1,4-poly-N-acetyl glucosamidinase, poly-beta-glucosaminidase

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About This Item

UNSPSC Code:
12352204
NACRES:
NA.54

Quality Level

specific activity

>200 USP units/mg solid

feature

DNA free

shipped in

wet ice

storage temp.

−20°C

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General description

Chitinase is an extracellular complex of enzymes that degrade chitin. Chitin is a cell wall component of Fungi and exoskeletal 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
The study of microbial communities has recently been revolutionized by the widespread adoption of culture- independent analytical techniques such as 16S rRNA gene sequencing and metagenomics. Since DNA contamination during sample preparation is a major problem of these sequence-based approaches, DNA extraction reagents free of DNA contaminants are essential. Purified Chitinase SAE0158 undergoes strict quality control testing to ensure the absence of detectable levels of contaminating DNA, using 35 cycles of PCR amplification of 16S and 18S rDNA, using universal primer sets.

Features and Benefits

This Chitinase is free of DNA contaminates, suitable for microbiome research. Cell walls digestion is performed safely by chitin degradation in fungi and other organisms.

Unit Definition

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.

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 3


Certificates of Analysis (COA)

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Rifat Hamid et al.
Journal of pharmacy & bioallied sciences, 5(1), 21-29 (2013-04-06)
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
Yuichiro Kezuka et al.
Journal of molecular biology, 358(2), 472-484 (2006-03-07)
Chitinase C (ChiC) from Streptomyces griseus HUT6037 was the first glycoside hydrolase family 19 chitinase that was found in an organism other than higher plants. An N-terminal chitin-binding domain and a C-terminal catalytic domain connected by a linker peptide constitute
T Tanabe et al.
Journal of bioscience and bioengineering, 89(1), 27-32 (2005-10-20)
A 49-kDa chitinase (pI7.3) was purified to homogeneity from the culture supernatant of Streptomyces griseus HUT 6037 by ultrafiltration, DEAE-Sephadex A-50 and Sephadex G-100 column chromatographies, and chromatofocusing. The purified enzyme was stable up to 40 degrees C. The N-terminal

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