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Bacillus sp. TS-23

Known as: Bacillus TS-23, Bacillus sp. (TS-23), Bacillus sp. strain TS-23 
 
National Institutes of Health

Papers overview

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2012
2012
The aim of this investigation was to synthesize the adipic acid-modified magnetic nanoparticles for the efficient immobilization… Expand
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2012
2012
Enzymes are highly complex systems with a substantial degree of structural variability in their folded state. In the presence of… Expand
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2010
2010
The role of the aspartate residues Asp193, Asp217, Asp228, Asp234, Asp236, Asp238, Asp438, and Asp461 of a truncated Bacillus sp… Expand
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2006
2006
The importance of 17 glutamate residues of a truncated Bacillus sp. strain TS-23 α-amylase (BACΔNC) was investigated by site… Expand
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2005
2005
The starch-binding domain of Bacillus sp. strain TS-23 α-amylase was introduced into the C-terminal end of Bacillus kaustophilus… Expand
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2004
2004
Bacillus stearothermophilus leucine aminopeptidase II (LAPII) was fused at its C-terminal end with the raw-starch-binding domain… Expand
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2003
2003
The methionine residues at positions 17, 104, 208, 214, 292, 315, 324, and 446 in the primary amino acid sequence of a truncated… Expand
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2003
2003
To understand the structure-function relationships of a truncated Bacillus sp. strain TS-23 α-amylase, each of His-137, His-191… Expand
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2002
2002
Abstract. The α-amylase from Bacillus sp. strain TS-23 is a secreted starch hydrolase with a domain organization similar to that… Expand
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2001
2001
A truncated Bacillus sp. TS-23 α-amylase gene lacking 96 and 294 bp at its 5′ and 3′ end respectively was prepared by polymerase… Expand
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