書誌事項
- タイトル別名
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- Improvement of Thermostability of a Calcium-free .ALPHA.-Amylase from an Alkaliphilic Bacillus sp. by Protein Engineering.
- Improvement of Thermostability of a Calcium-free α-Amylase from an Alkaliphilic Bacillus sp. by Protein Engineering
- Improvement of Thermostability of a Calcium free アルファ Amylase from an Alkaliphilic Bacillus sp by Protein Engineering
この論文をさがす
説明
A novel α-amylase (AmyK38) from an alkaliphilic Bacillus designated KSM-K38 is strongly resistant to chelators and oxidative reagents and contains no calcium. However, thermostabilization of AmyK38 is essential if it is to have industrial applications. Several chimeric enzymes between AmyK38 and the thermostable Arg181-G1y182-deleted mutant (dRG) of an α-amylase AmyK were constructed. A chimeric enzyme containing the N-terminal 21 amino acid residues of dRG was found to have higher thermostability than the parental AmyK38. By site-directed mutagenesis, AmyK38 was successfully thermostabilized by the single substitution of Tyrl1 by Phe without any changes in the kinetic features.
収録刊行物
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- Journal of Applied Glycoscience
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Journal of Applied Glycoscience 49 (3), 281-289, 2002
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
- 1390282681268724096
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- NII論文ID
- 10009257101
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- NII書誌ID
- AN10453916
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- ISSN
- 13403494
- 18807291
- 13447882
- http://id.crossref.org/issn/13447882
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- COI
- 1:CAS:528:DC%2BD38Xms1Smt78%3D
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- NDL書誌ID
- 6254302
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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
- IRDB
- NDL
- Crossref
- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可