Partial Purification and Characterization of an Acid Phosphatase from Papaya
- 1 September 1982
- journal article
- research article
- Published by Wiley in Journal of Food Science
- Vol. 47 (5) , 1498-1500
- https://doi.org/10.1111/j.1365-2621.1982.tb04969.x
Abstract
A phosphatase in papaya was extracted, partially purified, and characterized. With p‐nitrophenyl phosphate as substrate, the enzyme had a pH optimum of 6.0, which categorized it as an acid phosphatase, a temperature optimum of 37°C, and a Km of 1.0 mM. Heat inactivation of papaya acid phosphatase was biphasic, and the kinetics of both phases were first order reactions. D values at 60°, 65°, 70°C for the heat resistant phase were 21.0, 11.7, and 4.0 min, respectively. For the heat labile and heat resistant isozymes of papaya acid phosphatase, the activation energies, Ea, for thermal inactivation were 60.0 Kcal/mole and 37.8 Kcal/mole, respectively. The apparent molecular weight of the enzyme as determined by gel filtration was 120,000 daltons.This publication has 8 references indexed in Scilit:
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