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
MDL number:
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
Related Categories
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).
View more information on enzymes for complex carbohydrate analysis at www.sigma-aldrich.com/enzymeexplorer
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.
signalword
Danger
hcodes
pcodes
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
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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)
Chitosanase from Streptomyces griseus.
A Ohtakara
Methods in enzymology, 161, 505-510 (1988-01-01)
Georg Kopplin et al.
RSC advances, 11(23), 13780-13798 (2022-04-16)
Three alginates with fundamentally different block structures, poly-M, poly-G, and poly-MG, have been investigated upon ionic crosslinking with chitosan oligosaccharides (CHOS), using circular dichroism (CD), rheology, and computer simulations, supporting the previously proposed gelling principle of poly-M forming zipper-like junction
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