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Cloning, high-level expression and enzymatic properties of an intracellular serine protease from Bacillus sp. WRD-2

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Title Cloning, high-level expression and enzymatic properties of an intracellular serine protease from Bacillus sp. WRD-2
 
Creator An, Sun-Young
Ok, Min
Kim, Ji-Youn
Jang, Moon-Sun
Cho, Young-Su
Choi, Yong-Lark
Kim, Cheorl-Ho
Lee, Young-Choon
 
Subject Bacillus
Cloning
Overexpression
Intracellular serine protease
Purification
Recombinant enzyme
 
Description 141-147
A gene, isp-B, encoding an intracellular serine protease from a newly isolated Bacillus sp. WRD-2 was cloned and characterized. Nucleotide sequence analysis showed an open reading frame of 960 bp encoding a polypeptide comprised of 319 amino acids. The primary structure of the enzyme predicted the structural features characteristic of other intracellular serine proteases, including active sites, Ser, His and Asp, as well as no signal sequence. The predicted amino acid sequence showed more than 60% homology with the intracellular serine proteases from Bacillus species. When expressed in E. coli, the recombinant enzyme (rISP-B) was overproduced in the cytoplasm as soluble and active form. The purified enzyme was completely inhibited by phenylmethylsulfonyl fluoride, EDTA and antipain. The enzyme showed maximum activity at pH 8.0 and 45ºC. It was stable at pH from 7.5 to 11.0 and below 50ºC.
 
Date 2009-04-02T06:32:11Z
2009-04-02T06:32:11Z
2004-08
 
Type Article
 
Identifier 0301-1208
http://hdl.handle.net/123456789/3711
 
Language en_US
 
Publisher CSIR
 
Source IJBB Vol. 41(4) [August 2004]