57620
Inulinase from Aspergillus niger
lyophilized, powder, brown-gray, ~25 U/mg
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About This Item
Recommended Products
biological source
Aspergillus niger
Quality Level
form
powder
quality
lyophilized
specific activity
~25 U/mg
color
brown-gray
storage temp.
2-8°C
General description
Inulinases are classified as exoinulinases and endoinulinases.
Application
Inulinase from Aspergillus niger has been used as a glycoside hydrolase (GH) to study its potential to disperse bacteria (P. aeruginosa and S. aureus) from microbial biofilms using a polymicrobial well-plate model.
Biochem/physiol Actions
Inulinase is used in high-fructose syrup, which has therapeutic applications. Inulinase is reported to have high activity toward sucrose.
Inulinase hydrolyses inulin to produce oligosaccharides and liberate fructose. It also splits the terminal fructose units into sucrose and raffinose.
Unit Definition
1 U corresponds to the amount of enzyme which releases 1 μmol of reducing sugar (measured as fructose) per minute at pH 4.1 and 37°C from inulin
Other Notes
Characterization
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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R. Azhari et al.
Biotechnology and Applied Biochemistry, 11, 105-105 (1989)
Shuguang Yuan et al.
PloS one, 7(5), e37453-e37453 (2012-06-05)
Glycoside hydrolases of families 32 (GH32) and 68 (GH68) belong to clan GH-J, containing hydrolytic enzymes (sucrose/fructans as donor substrates) and fructosyltransferases (sucrose/fructans as donor and acceptor substrates). In GH32 members, some of the sugar substrates can also function as
Jenny Pouyez et al.
Biochimie, 94(11), 2423-2430 (2012-07-04)
Endo-inulinase is a member of glycosidase hydrolase family 32 (GH32) degrading fructans of the inulin type with an endo-cleavage mode and is an important class of industrial enzyme. In the present study, we report the first crystal structure of an
Ozden Canli et al.
Toxicology and industrial health, 28(10), 894-900 (2011-11-15)
This study evaluates the application of low magnetic field (LMF) on inulinase enzyme production by Geotrichum candidum under solid state fermentation (SSF) using leek as potential carbon source. First, the fermentation conditions were optimized using normal magnetic field grown microorganism.
Tohru Kobayashi et al.
Applied and environmental microbiology, 78(7), 2493-2495 (2012-01-31)
An inulinase-producing Microbulbifer sp. strain, JAM-3301, was isolated from a deep-sea sediment. An inulin operon that contained three open reading frames was cloned and sequenced. Two of the three genes were expressed. One product was an endo-inulinase, and the other
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