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ISOLATION AND CHARACTERIZATION OF A β‐FRUCTOFURANOSIDASE FROM PAPAYA
Author(s) -
CHAN HARVEY T.,
KWOK SIMON C. M.
Publication year - 1976
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1976.tb00609.x
Subject(s) - invertase , enzyme , sucrose , chemistry , substrate (aquarium) , size exclusion chromatography , kinetics , chromatography , biochemistry , food science , biology , ecology , physics , quantum mechanics
An 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 275,000.