The Inactivation kinetics of α-glucosidase, glucoamylase, α-amylase, and acid carboxypeptidase in fresh sake using a continuous flow system for high-pressure carbonation were investigated. In addition, the effects of ethanol and sugar concentrations on inactivation of the enzymes in high-pressure carbonated sake were investigated. Among the enzymes investigated, α-glucosidase was the most stable and α-amylase was the most labile on inactivation under carbonation. The decimal reduction times (D values) of α-glucosidase, glucoamylase, α-amylase (extrapolated from the Z value), and acid carboxypeptidase were 29, 6, 2, and 5 min respectively at 45°C. These values are lower than those subjected to heat treatment. On the carbonation treatment as well as the heat treatment, ethanol accelerated the inactivation of all four enzymes, but glucose depressed the inactivation of these enzymes, except for acid carboxypeptidase. These results suggest that this continuous flow system enabled effective inactivation of enzymes in fresh sake.
All Science Journal Classification (ASJC) codes
- Analytical Chemistry
- Applied Microbiology and Biotechnology
- Molecular Biology
- Organic Chemistry