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The heat stability and isoenzyme composition of peroxidases in Ohane grapes
Author(s) -
ROBINSON D. S.,
BRETHERICK M. R.,
DONNELLY JUDITH K.
Publication year - 1989
Publication title -
international journal of food science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.831
H-Index - 96
eISSN - 1365-2621
pISSN - 0950-5423
DOI - 10.1111/j.1365-2621.1989.tb00687.x
Subject(s) - peroxidase , isoelectric focusing , isoelectric point , chemistry , isozyme , composition (language) , pi , heat stability , biochemistry , specific activity , enzyme , chromatography , food science , philosophy , linguistics , materials science , composite material
Summary Soluble and ionically bound peroxidases have been obtained from homogenized Ohane grapes. The soluble fraction contained the highest level of peroxidase activity and accounted for approximately 87% of the total enzymic activity. Plots of the percentage of heat inactivation for the grape peroxidases against time were non‐linear with approximately 90% of the peroxidase activity being destroyed after 10 min at 80°C. Following heat inactivation there was no significant regeneration of enzymic activity. Using isoelectric focusing six isoperoxidases with isoelectric points ranging from approximately pI 3.5 to 9.8 were detected.