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Merck
CN

C9830

Chitosanase from Streptomyces griseus

lyophilized powder, >50 units/mg protein (Bradford)

Synonym(s):

Chitosan N-acetylglucosaminohydrolase

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About This Item

CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
MDL number:
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Product Name

Chitosanase from Streptomyces griseus, lyophilized powder, >50 units/mg protein (Bradford)

form

lyophilized powder

specific activity

>50 units/mg protein (Bradford)

purified by

chromatography

solubility

H2O: soluble, clear to slightly hazy, colorless (10U/0.3mL)

foreign activity

chitinase <1.0 units/mg protein

storage temp.

−20°C

Quality Level

Application

Chitosanase from Streptomyces griseus has been used in a study to assess the effect of chitin sources on production of chitinase and chitosanase. Chitosanase from Streptomyces griseus has also been used in a study to investigate the effective production of chitinase and chitosanase by Streptomyces griseus HUT 6037 using colloidal chitin and various degrees of deacetylation of chitosan.
Chitosanase from Streptomyces griseus has been used in the digestion of lacrimal gland (LG) tissues.
The enzyme from Sigma has been used for the hydrolysis of the crude cell wall preparation of oomycete Aphanomyces euteiches, a major parasite of legume plants. It has also been used for the enzymatic hydrolysis of the fully de-N-acetylated chitosan to get chitosan oligomer mixtures during the preparation of biocompatible chitosan-alginate gel.

Biochem/physiol Actions

Chitosanase catalyzes the endohydrolysis of N-acetylated chitosan specifically at the of β(1,4) linkages between N-acetyl-D-glucosamine and D-glucosamine residues. Chitosanase from Streptomyces griseus is capable of hydrolyzing both chitosan and carboxymethyl cellulose. Chitosanase is found in several types of microorganisms and is used for the lysis of fungal cell walls.

General description

Chitosanase is synthesized from Streptomyces griseus as an extracellular secreted enzyme and corresponds to a molecular weight of 34 kDa. It has a temperature and pH optimum of 60°C and 5.7, respectively. Chitosanase belongs to the glycosyl hydrolase family and comprises α-helical tertiary structure similar to lysozyme with substrate-binding cleft placed between two lobes.

Other Notes

One unit will release 1 μmole of glucosamine from chitosan per min at pH 5.0 at 37 °C as measured in the fluorimetric assay of Osswald, et al. (1992).

Physical form

Lyophilized powder containing potassium phosphate buffer salts

Preparation Note

For long term solution storage, reconstitute vial with 50% glycerol solution. Dilute to working concentrations with a 0.1% BSA solution.

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Regulatory Information

常规特殊物品
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Regulating temporospatial dynamics of morphogen for structure formation of the lacrimal gland by chitosan biomaterials
Hsiao YC and Yang TL
Biomaterials, 113, 42-55 (2017)
Ilham Badreddine et al.
Eukaryotic cell, 7(11), 1980-1993 (2008-09-23)
Chitin is an essential component of fungal cell walls, where it forms a crystalline scaffold, and chitooligosaccharides derived from it are signaling molecules recognized by the hosts of pathogenic fungi. Oomycetes are cellulosic fungus-like microorganisms which most often lack chitin
Effective production of chitinase and chitosanase by Streptomyces griseus HUT 6037 using colloidal chitin and various degrees of deacetylation of chitosan
Jung HS, et al.
Biotechnology and Bioprocess Engineering: BBE, 4(1), 26-31 (1999)
Thang Trung Khong et al.
Biomacromolecules, 14(8), 2765-2771 (2013-06-29)
Biocompatible hydrogels are very interesting for applications in, e.g., tissue engineering and for immobilization of cells, such as calcium-alginate gels where the calcium ions form specific interactions with the guluronic acid units. We here report on a new gelling system
Chitosanase from Streptomyces griseus.
A Ohtakara
Methods in enzymology, 161, 505-510 (1988-01-01)

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