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Biotechnology Section, Vitamins and Fine Chemicals Division, F. Hoffmann-La Roche AG, CH-4070 Basel, Switzerland
ABSTRACT
Phytases catalyse the hydrolysis of phytate (myo-inositol hexakisphosphate) to myo-inositol and inorganic phosphate. In this study genes encoding novel phytases from two different filamentous fungi, Aspergillus terreus strain 9A-1 and Myceliophthora thermophila were isolated. The encoded PhyA phytase proteins show 60% (A. terreus) and 48% (M. thermophila) identity, respectively, to the PhyA of Aspergillus niger and have 21-29% identity compared to other histidine acid phosphatases. All three PhyA proteins, in contrast to the A. niger pH 2.5-optimum acid phosphatase, prefer phytic acid as substrate and show enzyme activity at a broad range of acidic pH values. Based on their enzyme characteristics and protein sequence homology, the phytases form a novel subclass of the histidine acid phosphatase family.
1Author for correspondence: Adolphus P. G. M. van Loon. Tel: +41 61 688 7027. Fax: +41 61 688 1645.
Present address: Life Systems Design, Kundmannweg 2A, CH-4147 Aesch, Switzerland.
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