Dr fimbriae coding region associated hemolytic activity of Escherichia coli |
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| Authors: | PawelGoluszko StellaNowicki Anil KKaul TuanPham Bogdan JNowicki |
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| Institution: | International Center of Cooperative Research in Biotechnology, Faculty of Engineering, Osaka University, Suita, Osaka 565, Japan; Department of Chemical Process Engineering, Faculty of Engineering, Hokkaido University, Nishi 8-chome, Kita 13-jo, Sapporo 060, Japan |
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| Abstract: | Abstract Escherichia coli LE392 (pAL28) was previously isolated as a positive clone harboring the alginate lyase gene ( aly ) from an alginate-degrading strain, Pseudomonas sp. OS-ALG-9. The plasmid pAL205, one of the constructs obtained after successive subcloning of pAL28, gave the highest expression of aly in E. coli cells. A 8-fold increase in the alginate lyase (Aly) activity in E. coli JM109 (pAL205) was induced with isopropyl-β-d-thiogalactoside, which was 210 times higher than that in E. coli LE392 (pAL28). The highly significant increase in the expression of the Aly enzyme with pAL205 was investigated through the nucleotide sequence around the 5' region of aly as well as the N -terminal sequence of the purified enzyme. It was found that the Aly expressed in E. coli (pAL205) was a fused protein containing 7 residues from the N -terminus of β-galactosidase α-peptide and the mature protein found in the Pseudomonas sp. except for three residues in the N -terminal. |
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| Keywords: | Alginate lyase Gene expression Pseudomonas sp Fused protein Escherichia coli |
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