Isolation and characterization of a novel phytase from Penicillium simplicissimum
Jazyk angličtina Země Spojené státy americké Médium print
Typ dokumentu časopisecké články
PubMed
11271818
DOI
10.1007/bf02817409
Knihovny.cz E-zdroje
- MeSH
- 6-fytasa chemie izolace a purifikace metabolismus MeSH
- chromatografie iontoměničová MeSH
- elektroforéza v polyakrylamidovém gelu MeSH
- gelová chromatografie MeSH
- ionty farmakologie MeSH
- koncentrace vodíkových iontů MeSH
- kovy farmakologie MeSH
- molekulová hmotnost MeSH
- Penicillium enzymologie MeSH
- půdní mikrobiologie MeSH
- substrátová specifita MeSH
- teplota MeSH
- ultrafiltrace MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- 6-fytasa MeSH
- ionty MeSH
- kovy MeSH
Eighty-three isolates from different soil samples exhibited the potential for producing active extracellular phytase. The most active fungal isolate with phytase activity was identified as Penicillium simplicissimum. In shaking culture with enrichment medium, the highest extracellular phytase activity of the producing strain was 3.8 U/mL. The crude enzyme filtrate was purified to homogeneity using ultrafiltration. IEC and gel filtration chromatography. The molar mass of the purified enzyme was estimated to be 65 kDa on SDS-PAGE. The saccharide identification with periodic acid-Schiff reagent (PAS) and activity recognition by 1-naphthyl phosphate was all positive. The isoelectric point of the enzyme, as deduced by isoelectric focusing, was pH 5.8, the optimum pH and temperature being pH 4.0 and 55 degrees C, respectively. The purified enzyme revealed broad substrate specificity and was strongly inhibited by Fe2+, Fe3+ and Zn2+; however, no inhibition was found by EDTA and PMSF. Phytase activity was inhibited when 2 mmol/L of dodecasodium phytate was added and the Km for it was determined to be 813 mmol/L.
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