The role of acid phosphatase activity during enzymic dephosphorylation of phytates by Aspergillus niger phytase

Abstract

Acid phosphatase present in preparations of Aspergillus niger phytase accelerated dephosphorylation of sodium phytate. Its influence on the reaction rate and distribution of myo-inositol phosphates was most apparent at low pH value (2.5) and when acid-hydrolysed substrate was de-esterified enzymatically. With partly purified phytase, the predominant inositol form was tetraphosphate but a preparation having acid phosphatase activity caused an even distribution of lower inositol phosphates after a few hours. © 1993 Rapid Communications of Oxford Ltd.