Premium
Immobilized α‐amylase from Bacillus licheniformis : a potential enzymic time—temperature integrator for thermal processing
Author(s) -
CORDT SUSANNA DE,
HENDRICKX MARC,
MAESMANS GEERT,
TOBBACK PAUL
Publication year - 1992
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.1365-2621.1992.tb01236.x
Subject(s) - bacillus licheniformis , activation energy , isothermal process , thermodynamics , chemistry , integrator , amylase , atmospheric temperature range , order of reaction , kinetic energy , reaction rate constant , kinetics , analytical chemistry (journal) , materials science , chromatography , biochemistry , enzyme , physics , biology , genetics , quantum mechanics , voltage , bacillus subtilis , bacteria
Summar Biphasic and nth‐order models were tested as to their usefulness to fit experimental inactivation data of Bacillus licheniformis α‐amylase, immobilized on glass beads, and were discussed with respect to their suitability to characterize the considered enzymic system as a time—temperature integrator (TTI) to evaluate heat processes. Both isothermal and non‐isothermal inactivation experiments were carried out. Model (kinetic) parameters (rate constant k, activation energy E A and reaction order n) were estimated using a non‐linear regression procedure. The results obtained, especially the activation energy of about 293 kJ mole –1 , indicated a potential use of this system as a TTI for heating processes in the temperature range of 96–108°C.