Presented at the 43rd Annual Meeting of the Inst. of Food Technologists, New Orleans, LA, June 19–22, 1983.
Characterization of Soluble and Bound Peroxidases in Green Asparagus
Version of Record online: 25 AUG 2006
Journal of Food Science
Volume 48, Issue 5, pages 1412–1417, September 1983
How to Cite
WANG, Z. and LUH, B. S. (1983), Characterization of Soluble and Bound Peroxidases in Green Asparagus. Journal of Food Science, 48: 1412–1417. doi: 10.1111/j.1365-2621.1983.tb03504.x
- Issue online: 25 AUG 2006
- Version of Record online: 25 AUG 2006
- Ms received 12/27/82; revised 6/6/83; accepted 6/13/83
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.