書誌事項
- タイトル別名
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- Improvement of the Thermal Stability of a Calcium-free, Alkaline .ALPHA.-Amylase by Site-directed Mutagenesis
- Improvement of the thermal stability of a calcium-free, alkaline α-amylase by site-directed mutagenesis
- Improvement of the thermal stability of a calcium free alkaline a amylase by site directed mutagenesis
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抄録
Alkaline α-amylase from Bacillus sp. strain KSM-K38 (AmyK38) is a calcium-free enzyme that is stable against chelating and oxidative reagents. Recently, the thermostability of this enzyme was improved by replacement of its amino-terminal 11 amino acid residues with the corresponding residues of α-amylase from Bacillus sp. strain KSM-1378. In this study, to further improve the thermal stability, we compared the three-dimensional structure of AmyK38 with that of a hyper-thermostable α-amylase from Bacillus licheniformis. Using site-directed mutagenesis, we created a new possible ionic interaction in the flexible loop region from Gln167 to Gln170 of AmyK38 because the corresponding region in α-amylase from B. licheniformis has an ionic interaction between Glu167 and Lys170. Substitution of Gln167 or Tyr169 with Glu or Lys, respectively, was found to enhance the thermostability of AmyK38. Combination of both substitutions with replacement of the amino-terminal 11 residues further improved the thermostability of the enzyme.
収録刊行物
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- Journal of Applied Glycoscience
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Journal of Applied Glycoscience 54 (2), 77-83, 2007
日本応用糖質科学会
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詳細情報 詳細情報について
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- CRID
- 1390282681270456064
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- NII論文ID
- 10018617400
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- NII書誌ID
- AN10453916
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- ISSN
- 18807291
- 13447882
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- NDL書誌ID
- 8827830
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- NDL
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- 抄録ライセンスフラグ
- 使用不可