Characterization of barley enzymes involved in the lipid oxidation and the flavor stability of beer.
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- Kuroda Hisao
- Frontier Laboratories of Value Creation, SAPPORO BREWERIES LTD.
Bibliographic Information
- Other Title
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- ビール老化に関与するオオムギの脂質酸化酵素の研究
Description
In brewing, 2(E)-nonenal is considered to be the major contributor to the cardboard flavor that arises when a beer is stored for a prolonged period. We found that lipoxygenase-1, fatty acid hydroperoxide lyase (HPL) and 3Z:2E- isomerase in malt are involved in the production of 2(E)-nonenal. In this cascade pathway, linoleic acid from malt is transformed into linoleic acid 9-hydroperoxide (9-HPOD), and then 9-HPOD is cleaved into 3(Z)-nonenal, and finally 3(Z)-nonenal is isomerized to 2(E)-nonenal. These HPL and 3Z:2E-isomerase found in malt were the first enzymes appeared in monocots. We screened candidate barley EST and cloned a full length cDNA that code for this type of HPL, and designated as HvHPL2. Recombinant protein of HvHPL2 cleaved both 9-HPOD and linoleic acid 13-hydroperoxide, indicating HvHPL2 belongs to CYP74C subfamily of cytochrome P450. Flavor stability of beer could be improved by developing barley mutant lines of HvHPL2.
Journal
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- Plant and Cell Physiology Supplement
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Plant and Cell Physiology Supplement 2006 (0), S011-S011, 2006
The Japanese Society of Plant Physiologists
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Details 詳細情報について
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- CRID
- 1390282680607873024
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- NII Article ID
- 130006992224
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- Data Source
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- JaLC
- CiNii Articles
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- Abstract License Flag
- Disallowed
