R. Srivastava et al., PURIFICATION AND CHARACTERIZATION OF AN ACID-PHOSPHATASE FROM ARACHIS-HYPOGAEA, Biochemistry and molecular biology international, 35(5), 1995, pp. 949-956
An acid phosphatase from Arachis hypogaea ( peanuts) has been purified
. The electrophoretically homogeneous enzyme preparation is free of an
y phophodiesterase activity. The enzyme has a molecular weight of 120,
000. Among the various phosphomonoesters tested, p-nitrophenylphosphat
e was found to be its most effective substrate. The K-m for p-nitrophe
nylphosphate was 1.21 mM at pH 5.0 and 25 degrees C. The enzyme was th
ermostable and did not loose activity after 1 hr at 50 degrees C.