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Orientador(es)
Resumo(s)
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.
Descrição
Palavras-chave
Biocatalysis Enzyme thermal inactivation Time-temperature integrators Water activity
Contexto Educativo
Citação
SARAIVA, Jorge [et al] - Inactivation kinetics of horseradish peroxidase in organic solvents of different hydrophobicity at different water contents. International Journal of Food Science and Technology. ISSN 0950-5423. 31:3 (1996) 233-240
Editora
Wiley Blackwell