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.
Actions biochimiques/physiologiques
Inulinase hydrolyses inulin to produce oligosaccharides and liberate fructose. It also splits the terminal fructose units into sucrose and raffinose.
Inulinase is used in high-fructose syrup, which has therapeutic applications. Inulinase is reported to have high activity toward sucrose.
Définition de l'unité
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
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
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.
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
Applied microbiology and biotechnology, 96(6), 1517-1526 (2012-05-25)
A novel extracellular exoinulinase was purified and characterized from a new yeast strain KRF1(T), and the gene encoding the enzyme was successfully cloned. The enzyme was stable at low pH between 3.0 and 6.5. The K (m) and V (max)
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