Isolation and characterization of a novel phytase from Penicillium simplicissimum
Language English Country United States Media print
Document type Journal Article
PubMed
11271818
DOI
10.1007/bf02817409
Knihovny.cz E-resources
- MeSH
- 6-Phytase chemistry isolation & purification metabolism MeSH
- Chromatography, Ion Exchange MeSH
- Electrophoresis, Polyacrylamide Gel MeSH
- Chromatography, Gel MeSH
- Ions pharmacology MeSH
- Hydrogen-Ion Concentration MeSH
- Metals pharmacology MeSH
- Molecular Weight MeSH
- Penicillium enzymology MeSH
- Soil Microbiology MeSH
- Substrate Specificity MeSH
- Temperature MeSH
- Ultrafiltration MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- 6-Phytase MeSH
- Ions MeSH
- Metals 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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