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Hyperalkaline and thermostable phosphatase inThermus thermophilus

Hyperalkaline and thermostable phosphatase inThermus thermophilus The phosphatases existing in the extreme thermophilic bacteriumThermus thermophilus have been studied. Utilizing ion exchange, hydrophobic, pseudoaffinity, and affinity chromatography, a number of distinct phosphatase activities were identified. At least four phosphatases, with optimum pH ranging between 5.0 and 11.5, were assayed withp-nitrophenylphosphate, and two with optimum pH between 7.0 and 11.0, with32P-casein as substrate. The authors have focused on the hyperalkaline phosphatase and have tried to purify and characterize it. This hyperalkaline phosphatase reaches a maximal level at the stationary phase of the growth, and is co-purified with alkaline phosphatase with optimum pH of 10.2. The enzymes present a relative mol wt of 65 and 58 kDa, respectively, as judged by SDS-PAGE and Sephadex G-150 column, and possess similar properties, indicating that they are isoforms. These enzymes barely function in the presence of tartrate, and are inhibited by EDTA, pyrophosphate, and molybdate. Among the metals tested, Hg2+ appeared as the strongest inhibitor of the hyperalkaline phosphatase. The two enzymes are thermostable and, upon treatment at 90°C for 10 min, 75% of their activity remains. The physiological role and function of these phosphatases need further investigation. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Applied Biochemistry and Biotechnology Springer Journals

Hyperalkaline and thermostable phosphatase inThermus thermophilus

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References (23)

Publisher
Springer Journals
Copyright
Copyright © 1999 by Humana Press Inc.
Subject
Chemistry; Biotechnology; Biochemistry, general
ISSN
0273-2289
eISSN
1559-0291
DOI
10.1007/BF02787778
Publisher site
See Article on Publisher Site

Abstract

The phosphatases existing in the extreme thermophilic bacteriumThermus thermophilus have been studied. Utilizing ion exchange, hydrophobic, pseudoaffinity, and affinity chromatography, a number of distinct phosphatase activities were identified. At least four phosphatases, with optimum pH ranging between 5.0 and 11.5, were assayed withp-nitrophenylphosphate, and two with optimum pH between 7.0 and 11.0, with32P-casein as substrate. The authors have focused on the hyperalkaline phosphatase and have tried to purify and characterize it. This hyperalkaline phosphatase reaches a maximal level at the stationary phase of the growth, and is co-purified with alkaline phosphatase with optimum pH of 10.2. The enzymes present a relative mol wt of 65 and 58 kDa, respectively, as judged by SDS-PAGE and Sephadex G-150 column, and possess similar properties, indicating that they are isoforms. These enzymes barely function in the presence of tartrate, and are inhibited by EDTA, pyrophosphate, and molybdate. Among the metals tested, Hg2+ appeared as the strongest inhibitor of the hyperalkaline phosphatase. The two enzymes are thermostable and, upon treatment at 90°C for 10 min, 75% of their activity remains. The physiological role and function of these phosphatases need further investigation.

Journal

Applied Biochemistry and BiotechnologySpringer Journals

Published: Dec 14, 2007

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