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

Abstract:

:An extracellular acid phosphatase isolated from the culture of a wild strain Aspergillus 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 and topt 66 degrees C. The acid phosphatase showed a wide substrate specificity and a high affinity for sodium phytate, 2.5x 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.

journal_title

Folia microbiologica

authors

Gargova S,Sariyska M,Angelov A,Stoilova I

doi

10.1007/BF02931618

subject

Has Abstract

pub_date

2006-01-01 00:00:00

pages

541-5

issue

6

eissn

0015-5632

issn

1874-9356

journal_volume

51

pub_type

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