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http://hdl.handle.net/10773/7735
Title: | Inactivation kinetics of horseradish peroxidase in organic solvents of different hydrophobicity at different water contents |
Author: | Saraiva, Jorge Oliveira, Jorge C. Oliveira, Susana Hendrickx, Marc |
Keywords: | Biocatalysis Enzyme thermal inactivation Time-temperature integrators Water activity |
Issue Date: | 1996 |
Publisher: | Wiley-Blackwell |
Abstract: | 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. |
Peer review: | yes |
URI: | http://hdl.handle.net/10773/7735 |
DOI: | 10.1046/j.1365-2621.1996.00343.x 10.1046/j.1365-2621.1996.00343.x |
ISSN: | 1365-2621 |
Appears in Collections: | QOPNA - Artigos |
Files in This Item:
File | Description | Size | Format | |
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P2_IJFST_Peroxidase organic solvents.pdf | 600.58 kB | Adobe PDF |
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