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.

• MeSH
• Aspergillus niger enzymologie   MeSH
• chromatografie iontoměničová MeSH
• gelová chromatografie MeSH
• koncentrace vodíkových iontů MeSH
• kyselá fosfatasa izolace a purifikace   metabolismus   MeSH
• kyselina fytová metabolismus   MeSH
• nitrofenoly metabolismus   MeSH
• organofosforové sloučeniny metabolismus   MeSH
• stabilita enzymů MeSH
• substrátová specifita MeSH
• teplota MeSH
• ultrafiltrace MeSH
• Publikační typ
• časopisecké články MeSH
• Názvy látek
• kyselá fosfatasa MeSH
• kyselina fytová MeSH
• nitrofenoly MeSH
• nitrophenylphosphate MeSH Prohlížeč
• organofosforové sloučeniny MeSH