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Inhibition of Polyphenoloxidase by Sulfite
Author(s) -
SAYAVEDRASOTO L. A.,
MONTGOMERY M. W.
Publication year - 1986
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.1365-2621.1986.tb13852.x
Subject(s) - sulfite , chemistry , chromatography , sodium sulfite , gel electrophoresis , column chromatography , catechol , pear , biochemistry , organic chemistry , sodium , botany , biology
When polyphenoloxidase (PPO) was exposed to sulfite prior to susbstrate addition, inhibition was irreversible. Trials to regenerate PPO activity, using extensive dialysis, column chromatography, and addition of copper salts were not successful. Increased concentrations of sulfite and pH levels less than 5 enhanced the inhibition of PPO by sulfite. At pH 4, concentrations greater than 0.04 mg/mL completely inhibited 1,000 units of PPO activity almost instantaneously. This suggested that the HSO 3 ‐ molecule was the main component in the sulfite system inhibiting PPO. Column chromatography, extensive dialysis, and gel electrophoresis did not demonstrate 35 SO 2 bound to purified pear PPO protein. Formation of extra protein bands of sulfite inhibited purified pear PPO fractions on gel electrophoresis was demonstrated. This and other evidence suggested that the major mode of direct irreversible inhibition of PPO was modification of the protein structure, with retention of its molecular unity.