Aspergillus niger pH 2.1 optimum acid phosphatase with high affinity for phytate
| Autor: | I. Stoilova, S. Gargova, Angel Angelov, M.V. Sariyska |
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| Rok vydání: | 2006 |
| Předmět: |
Phytic Acid
Acid Phosphatase Size-exclusion chromatography Ion chromatography Ultrafiltration Microbiology Substrate Specificity Nitrophenols chemistry.chemical_compound Organophosphorus Compounds Enzyme Stability chemistry.chemical_classification Chromatography biology Aspergillus niger Temperature Acid phosphatase General Medicine Hydrogen-Ion Concentration Chromatography Ion Exchange Phosphate biology.organism_classification Ultrafiltration (renal) Enzyme chemistry Sephadex Chromatography Gel biology.protein |
| Zdroj: | Folia Microbiologica. 51:541-545 |
| ISSN: | 1874-9356 0015-5632 |
| DOI: | 10.1007/bf02931618 |
| Popis: | An extracellular acid phosphatase isolated from the culture of a wild strainAspergillus niger, producing the dephosphorylating 3-phytase, was obtained in a homogeneous form by sequential application of ultrafiltration through PS 50 membrane, gel filtration on Sephadex G-100 and ion exchange chromatography on DEAE-Sepharose CL 6B and CM-Sepharose CL 6B. The enzyme showed a maximum catalytic value in a strongly acidic range (pH 2.0–2.4) with pHopt 2.1 andt opt 66 °C. The acid phosphatase showed a wide substrate specificity and a high affinity for sodium phytate, 2.5× higher than with 4-nitrophenyl phosphate. This property of the acid phosphatase demonstrated that it is a potent 3-phytase at pH 2.1 and is of great significance for a practical application of the dephosphorylating complex — its addition to the diets of monogastric animals in view of the low pH values in the digestive tract. |
| Databáze: | OpenAIRE |
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