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Applied and Environmental Microbiology, October 1999, p. 4682-4684, Vol. 65, No. 10
0099-2240/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Dephosphorylation of Phytate by Using the Aspergillus niger Phytase with a High Affinity for Phytate

Tadashi Nagashima,1,* Tatsuya Tange,1 and Hideharu Anazawa2

Research and Development, Shin Nihon Chemical Co., Ltd., Anjo, Aichi 446-0063,1 and Tokyo Research Laboratories, Kyowa Hakko Kogyo Co., Ltd., 3-6-6 Asahi-machi, Machida, Tokyo 194-8533,2 Japan

Received 8 March 1999/Accepted 29 June 1999

A phytase (EC 3.1.3.8) with a high affinity for phytic acid was found in Aspergillus niger SK-57 and purified to homogeneity in four steps by using ion-exchange chromatography (two types), gel filtration, and chromatofocusing. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the purified enzyme gave a single stained band at a molecular mass of approximately 60 kDa. The Michaelis constant of the enzyme for phytic acid (18.7 ± 4.6 µM) was statistically analyzed. In regard to the orthophosphate released from phytic acid, a significant difference between a low Km phytase from A. niger SK-57 and a high Km phytase from Aspergillus ficuum was recognized.

* Corresponding author. Mailing address: Shin Nihon Chemical Co., Ltd., Research and Development, 19-10 Showa-cho, Anjo, Aichi 446-0063, Japan. Phone: 81 566 76 5171. Fax: 81 566 75 0010. E-mail: nagashma{at}d1.dion.ne.jp.

Applied and Environmental Microbiology, October 1999, p. 4682-4684, Vol. 65, No. 10
0099-2240/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.




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