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Purification and Characterization of Peroxidase Isoenzymes from Green Peas (Pisum sativum)
Author(s) -
HALPIN B.,
PRESSEY R.,
JEN J.,
MONDY N.
Publication year - 1989
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.1365-2621.1989.tb04672.x
Subject(s) - guaiacol , peroxidase , pisum , isozyme , chemistry , cationic polymerization , ion chromatography , sativum , chromatography , cyanide , biochemistry , nuclear chemistry , enzyme , botany , organic chemistry , biology
Peroxidase isoenzymes were purified from green peas with ion‐exchange chromatography on DEAE‐ and S‐Sepharose. Three isoenzymes were identified, one neutral (N) and two cationic (C1, C2). N was extremely heat labile, with 50% original activity lost after heating 1.5 min at 25°C. N had Km values (pH 5.0) of 10.2 mM and 2.6 mM for guaiacol and H 2 O 2 , respectively. C1 and C2 retained activity on heating at 30–70°C. C1 was able to reactivate after thermal inactivation. Km values for guaiacol/H 2 O 2 were 10.8 mM/7.2 mM (pH 5.0) and 10.8 mM/4.3 mM (pH 6.0) for C1 and C2, respectively. The three isoenzymes exhibited different peroxidase activities with different H‐donors, different sensitivities to cyanide and different abilities to catalyze oxidation of indoleacetic acid.