Inactivation kinetics of horseradish peroxidase in organic solvents of different hydrophobicity at different water contents

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Inactivation kinetics of horseradish peroxidase in organic solvents of different hydrophobicity at different water contents

The thermal stability of horseradish peroxidase suspensions was studied in three organic solvents of different hydrophobicity (dodecane, octane, and 1-octanol) at three different water contents (14.1, 55.3 and 256.2 mg water g dry protein). In these conditions, the enzyme is much more stable than in aqueous solutions (inactivation temperatures were in the range of 125–1508C). The enzyme showed ...

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ژورنال

عنوان ژورنال: International Journal of Food Science and Technology

سال: 1996

ISSN: 0950-5423,1365-2621

DOI: 10.1046/j.1365-2621.1996.00343.x