Inactivation of Enzymes in Fresh Sake Using a Continuous Flow System for High-Pressure Carbonation

• Published in: Bioscience, biotechnology, and biochemistry Vol. 69; no. 11; pp. 2094 - 2100
• Main Authors: TANIMOTO, Shota, MATSUMOTO, Hideyuki, FUJII, Kazuyoshi, OHDOI, Ritsushi, SAKAMOTO, Koji, IZUWA, Shinya, YAMANE, Yuichi, MIYAKE, Masaki, SHIMODA, Mitsuya, OSAJIMA, Yutaka
• Format: Journal Article
• Language: English
• Published: Tokyo Japan Society for Bioscience, Biotechnology, and Agrochemistry 2005; Japan Society for Bioscience Biotechnology and Agrochemistry; Oxford University Press
• Subjects: Alcoholic Beverages; alpha-Amylases - metabolism; alpha-Glucosidases - metabolism; Bacteria - cytology; Bacteria - enzymology; Biological and medical sciences; Carbohydrates - pharmacology; Carbonates - pharmacology; Carboxypeptidase C; Cathepsin A - metabolism; Enzyme Stability; Enzymes; Ethanol; Ethanol - pharmacology; fresh sake; Fundamental and applied biological sciences. Psychology; Glucan 1,4-alpha-Glucosidase - metabolism; Glucoamylase; Glucose; Heat treatments; high-pressure carbonation; inactivation kinetics of enzymes; Kinetics; Microbial Viability; Pressure; Q1; Sake; Sugar; Continuous process; high-pressure carbonation; inactivation kinetics of enzymes: fresh sake; Enzyme; Kinetics; Inactivation; High pressure; Sake
• ISSN: 0916-8451; 1347-6947
• DOI: 10.1271/bbb.69.2094

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.