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Inactivation kinetics of horseradish peroxidase in organic solvents of different hydrophobicity at different water contents
Author(s) -
Saraiva Jorge,
Oliveira Jorge C.,
Oliveira Susana,
Hendrickx Marc
Publication year - 1996
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 - 10.1046/j.1365-2621.1996.00343.x
Subject(s) - chemistry , horseradish peroxidase , dodecane , octane , kinetics , solvent , aqueous solution , thermal stability , organic solvent , chromatography , organic chemistry , enzyme , chemical engineering , physics , quantum mechanics , engineering
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 256.2mg water g −1 dry protein). In these conditions, the enzyme is much more stable than in aqueous solutions (inactivation temperatures were in the range of 125–150°C). The enzyme showed a similar stability when in the presence of organic solvents, compared to the enzyme in a solid matrix without organic solvents with the same water content. The inactivation kinetics was well described by assuming the existence of two iso‐enzymes, both inactivating according to a First order model. The lowest value for the z‐value of both fractions (around 15°C) was obtained at the higher water content studied. The use of solvent and water content variables should be adequate to develop time‐temperature integrators to monitor thermal processes at 100–140°C.