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Characterization of Soluble and Bound Peroxidases in Green Asparagus
Author(s) -
WANG Z.,
LUH B. S.
Publication year - 1983
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.1365-2621.1983.tb03504.x
Subject(s) - peroxidase , asparagus , chemistry , isoelectric point , chromatography , isoelectric focusing , ammonium , fractionation , phosphate , sodium , phosphate buffered saline , hydrogen peroxide , enzyme , biochemistry , botany , organic chemistry , biology
Soluble and ionically bound peroxidases were extracted from green asparagus with 0.05M sodium phosphate (pH 7.0) and the same buffer containing 1.0M NaCl, respectively. The two forms of peroxidase have been purified 237 and 53 fold, respectively, through ammonium sulphate fractionation, and successive chromatography on Sephacryl S‐200 and ConA Sepharose 4B columns. Eleven isoenzymes with different pI values were detected from the soluble form using isoelectric focusing and eight from the ionically bound form. The two forms of perooxidase showed a similar optimum pH range of 4.2–5.0 using three kinds of hydrogen donor with different buffers. The optimum temperature of the two peroxidase forms at pH 4.5 was around 50°C. Heat inactivation of both forms at 70° and 90°C was observed to be biphasic.