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Purification and characterization of an acid phosphatase from Arachis hypogaea
R Srivastava1, Y S Rajput, S K Khare
1Chemistry Department I.I.T. Delhi, India.
Biochemistry and Molecular Biology International
|April 1, 1995
Abstract:
An acid phosphatase from Arachis hypogaea (peanuts) has been purified. The electrophoretically homogeneous enzyme preparation is free of any phophodiesterase activity. The enzyme has a molecular weight of 120,000. Among the various phosphomonoesters tested, p-nitrophenylphosphate was found to be its most effective substrate. The Km for p-nitrophenylphosphate was 1.21 mM at pH 5.0 and 25 degrees C. The enzyme was thermostable and did not loose activity after 1 hr at 50 degrees C.