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Purification and characterization of a lactonase from Erwinia cypripedii 314B that hydrolyzes (S)-5-oxo-2-tetrahydrofurancarboxylic acid
Authors:Kazuya?Mochizuki  author-information"  >  author-information__contact u-icon-before"  >  mailto:mochizuki-kazuya@aist.go.jp"   title="  mochizuki-kazuya@aist.go.jp"   itemprop="  email"   data-track="  click"   data-track-action="  Email author"   data-track-label="  "  >Email author
Affiliation:(1) Institute for Biological Resources and Functions, National Institute of Advanced Industrial Science and Technology, Tsukuba Central 6, 1-1-1 Higashi, 305-8566 Tsukuba, Ibaraki , Japan
Abstract:A bacterium, strain 314B, able to assimilate (S)-5-oxo-2-tetrahydrofurancarboxylic acid was isolated from soil and identified as Erwinia cypripedii. A lactonase hydrolyzing (S)-5-oxo-2-tetrahydrofurancarboxylic acid to l-agr-hydroxyglutaric acid was purified 63-fold with 2% recovery from crude extracts of this bacterium to homogeneity as judged by SDS-PAGE. The molecular masses estimated by SDS-PAGE and gel filtration were 41 kDa and 79 kDa, respectively. The maximum activity was observed at pH 6.5–7.5 and 35–45 °C. The enzyme showed lower activity toward dl-2-oxotetrahydrofuran-4,5-dicarboxylic acid, but did not act on (R)-5-oxo-2-tetrahydrofurancarboxylic acid and other natural and synthetic lactones tested.
Keywords:(S)-5-oxo-2-tetrahydrofurancarboxylic acid  Lactonase   Erwinia cypripedii 314B
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