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Aspergillus niger pH 2.1 optimum acid phosphatase with high affinity for phytate

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Abstract

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.

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Authors and Affiliations

  1. Department of Biotechnology, University of Food Technologies, 4002, Plovdiv, Bulgaria

    S. Gargova, M. Sariyska, A. Angelov & I. Stoilova

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  1. S. Gargova
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  2. M. Sariyska
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  3. A. Angelov
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  4. I. Stoilova
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Correspondence to S. Gargova.

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Gargova, S., Sariyska, M., Angelov, A. et al. Aspergillus niger pH 2.1 optimum acid phosphatase with high affinity for phytate. Folia Microbiol 51, 541–545 (2006). https://doi.org/10.1007/BF02931618

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  • DOI: https://doi.org/10.1007/BF02931618

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