Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 2094-2100 |
| Number of pages | 7 |
| Journal | Bioscience, Biotechnology and Biochemistry |
| Volume | 69 |
| Issue number | 11 |
| DOIs | |
| Publication status | Published - Dec 8 2005 |
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All Science Journal Classification (ASJC) codes
- Biotechnology
- Analytical Chemistry
- Biochemistry
- Applied Microbiology and Biotechnology
- Molecular Biology
- Organic Chemistry
Cite this
Inactivation of enzymes in fresh sake using a continuous flow system for high-pressure carbonation. / Tanimoto, Shota; Matsumoto, Hideyuki; Fujii, Kazuyoshi; Ohdoi, Ritsushi; Sakamoto, Koji; Izuwa, Shinya; Yamane, Yuichi; Miyake, Masaki; Shimoda, Mitsuya; Osajima, Yutaka.
In: Bioscience, Biotechnology and Biochemistry, Vol. 69, No. 11, 08.12.2005, p. 2094-2100.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Inactivation of enzymes in fresh sake using a continuous flow system for high-pressure carbonation
AU - Tanimoto, Shota
AU - Matsumoto, Hideyuki
AU - Fujii, Kazuyoshi
AU - Ohdoi, Ritsushi
AU - Sakamoto, Koji
AU - Izuwa, Shinya
AU - Yamane, Yuichi
AU - Miyake, Masaki
AU - Shimoda, Mitsuya
AU - Osajima, Yutaka
PY - 2005/12/8
Y1 - 2005/12/8
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=28244434368&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=28244434368&partnerID=8YFLogxK
U2 - 10.1271/bbb.69.2094
DO - 10.1271/bbb.69.2094
M3 - Article
C2 - 16306690
AN - SCOPUS:28244434368
VL - 69
SP - 2094
EP - 2100
JO - Bioscience, Biotechnology and Biochemistry
JF - Bioscience, Biotechnology and Biochemistry
SN - 0916-8451
IS - 11
ER -