ABSTRACTAn invertase in papaya was extracted, partially purified and characterized. Substrate specificity studies showed the enzyme to be a β‐fructo‐furanosidase. The enzyme has a pH optimum of 4.6 and a temperature optimum of 40° C. The Km of the enzyme, with sucrose as a substrate, was 7.7 mM. Heat inactivation of papaya invertase was biphasic, and the kinetics of both phases were first order. The activation energies for the thermal inactivation of the two phases were 33.5 kcal and 53.6 kcal. The enzyme's apparent molecular weight as determined by gel filtration was 27
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