DSC and protein–based time‐temperature integrators: Case study of α‐amylase stabilized by polyols and/or sugar

摘要: Differential scanning calorimetry (DSC) was used as a tool for rapid assay of the thermostability two Bacillus sp. alpha-amylases and horseradish peroxidase function concentration glycerol, sorbitol, sucrose. In this screening study, DSC peak temperature proved to be good measure protein thermostability. By means isothermal heating experiments, kinetics heat decay B. amyloliquefaciens alpha-amylase were studied by following course area (heat exchange (DeltaH/wt)) time. The high stability enzyme in presence polyolic alcohols or carbohydrates allowed working at temperatures 127 degrees C. results study can have particular relevance with regard research on development protein-based time-temperature integrators (TTls) evaluating pasteurization sterilization treatments foods pharmaceutical products. use (DeltaH.wt) TTI-response validated experiments time-variable profile. Finally, it shown how such non-isothermal even (re-) estimation kinetic parameters (k, E(A)). (c) 1994 John Wiley & Sons, Inc.