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ISOLATION AND CHARACTERIZATION OF CATALASE FROM PAPAYA
Author(s) -
CHAN HARVEY T.,
TAM STEVEN Y. T.,
KOIDE ROBIN T.
Publication year - 1978
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.1365-2621.1978.tb02468.x
Subject(s) - catalase , chemistry , enzyme , mole , size exclusion chromatography , kinetics , chromatography , biochemistry , physics , quantum mechanics
A catalase (I.U.B.1.11.1.6) in papaya was extracted, purified and characterized. The enzyme had a pH optimum of 6.1 and was stable when refrigerated or frozen. The enzyme was inactivated by acidification to pH 3.5. Heat inactivation of papaya catalase was biphasic at 55°C and 60°C, and monophasic at 65°C. Kinetics of both phases were first order. The activation energies for the thermal inactivation of the two phases were 85.9 Kcal/mole and 97.0 Kcal/mole. The apparent molecular weight of the enzyme as determined by gel filtration was 160,000. The unsuitability of papaya catalase as a biochemical indicator for heat inactivation is discussed.