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Inactivation of Polyphenoloxidase by Pulsed Light
Author(s) -
Manzocco Lara,
Panozzo Agnese,
Nicoli Maria Cristina
Publication year - 2013
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 - 10.1111/1750-3841.12216
Subject(s) - chemistry , enzyme , cleavage (geology) , kinetics , biophysics , enzyme assay , biochemistry , photochemistry , biology , paleontology , physics , quantum mechanics , fracture (geology)
The effect of pulsed light on the inactivation of polyphenoloxidase (PPO) in model solutions was investigated focusing on the effect of enzyme concentration and total energy dose of the treatment. PPO inactivation increased with the dose of the treatment. Complete enzyme inactivation was achieved by pulsed light doses higher than 8.75 J cm −2 . At low PPO concentrations (4 to 10 U), the enzyme resulted highly inactivated by pulsed light treatment. Further increase in enzyme units determined a progressive decrease in PPO inactivation. The latter was attributed to protein structural modifications including cleavage and unfolding/aggregation phenomena. PPO amounts higher than 10 U probably favoured enzyme conformations that were less prone to intermolecular rearrangements leading to inactivation.