P9792
Phytase from Aspergillus ficuum
lyophilized powder, 1-5 units/mg solid (as phosphatase activity)
Synonym(s):
3-Phytase, myo-Inositol-hexakisphosphate 3-phosphohydrolase
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About This Item
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form
lyophilized powder
specific activity
1-5 units/mg solid (as phosphatase activity)
storage temp.
−20°C
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Quality
May contain glucosidases and phosphatases.
Unit Definition
One unit will liberate 1.0 μmole of inorganic P from 4.2 × 10-2 M Mg·K phytate per min at pH 2.5 at 37 °C.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
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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Journal of bacteriology, 112(1), 434-438 (1972-10-01)
The fungus Aspergillus ficuum NRRL 3135 is known to produce an extracellular nonspecific orthophosphoric monoester phosphohydrolase (EC 3.1.3.2) with a pH optimum of 2.0, as well as an extracellular myo-inositol hexaphosphate phosphohydrolase (EC 3.1.3.8; phytase) with pH optima of 2.0
Journal of biotechnology, 85(1), 15-24 (2001-02-13)
Thermostability is a key feature for commercially attractive variants of the fungal enzyme phytase. In an initial set of experiments, we restored ionic interactions and hydrogen bonds on the surface of Aspergillus terreus phytase, which are present in the homologous
Bioorganic & medicinal chemistry letters, 15(12), 3157-3161 (2005-05-10)
A novel approach for measuring phytase activity is presented. We have developed a new chromophoric substrate analog of phytic acid, 5-O-[6-(benzoylamino)hexyl]-d-myo-inositol-1,2,3,4,6-pentakisphosphate that permits direct measurement of the phosphate ester bond-cleavage reaction using HPLC. This compound, along with its dephosphorylated T-phosphatidylinositol
Molecular and physiological characterisation of a 3-phytase from soil bacterium Klebsiella sp. ASR1.
Applied microbiology and biotechnology, 65(1), 110-118 (2004-01-17)
Klebsiella sp. strain ASR1 isolated from an Indonesian rice field is able to hydrolyse myo-inositol hexakis phosphate (phytate). The phytase protein was purified and characterised as a 42 kDa protein accepting phytate, NADP and sugar phosphates as substrates. The corresponding
Folia microbiologica, 45(2), 128-132 (2001-03-29)
Kinetics of phytate hydrolysis by Aspergillus niger phytase and correlation between the amount of released phosphate and creation of lower myo-inositol phosphates were investigated. Phytase was able to hydrolyze myo-inositol hexakis-, pentakis-, tetrakis-, and trisphosphates. Finally, about 56% of total
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