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Cloning, sequence analysis, and expression of a gene encoding an endoxylanase from Bacillus halodurans S7

Mamo, Gashaw LU ; Delgado, O ; Martinez, A ; Mattiasson, Bo LU and Hatti-Kaul, Rajni LU (2006) In Molecular Biotechnology 33(2). p.149-159
Abstract
The gene encoding an alkaline active xylanase of Bacillus halodurans S7, containing an open reading frame of 1188 nucleotides encoding 396 amino acids, was cloned and expressed in Escherchia coli. On the basis of sequence similarity, possible -10 and -35, ribosome binding, and transcription terminator regions were identified. Analysis of the deduced amino acid sequence revealed that the protein was a single domain enyzme belonging to family 10 and designated as xyn10A. The calculated molecular mass and isoelectric point (pI) of the mature peptide were 42.6 and 4.5 kDa, respectively. Xylanase acitivity expressed by the recombinant organism was detected in the cytoplasm, periplasm and the extracellular medium. In an 18-h old culture, about... (More)
The gene encoding an alkaline active xylanase of Bacillus halodurans S7, containing an open reading frame of 1188 nucleotides encoding 396 amino acids, was cloned and expressed in Escherchia coli. On the basis of sequence similarity, possible -10 and -35, ribosome binding, and transcription terminator regions were identified. Analysis of the deduced amino acid sequence revealed that the protein was a single domain enyzme belonging to family 10 and designated as xyn10A. The calculated molecular mass and isoelectric point (pI) of the mature peptide were 42.6 and 4.5 kDa, respectively. Xylanase acitivity expressed by the recombinant organism was detected in the cytoplasm, periplasm and the extracellular medium. In an 18-h old culture, about 39% of the xylanase was detected in the medium. The stability and activity profile of the recombinant xylanase was similar to the properties of the enzyme produced by the wild-type organism. (Less)
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author
; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
purification, expression, alkaliphile, endoxylanase, Bacillus halodurans
in
Molecular Biotechnology
volume
33
issue
2
pages
149 - 159
publisher
Humana Press
external identifiers
  • wos:000238071400007
  • scopus:33745698009
ISSN
1559-0305
language
English
LU publication?
yes
id
6abce049-5161-4773-aba0-ac6fc74c3c1b (old id 407368)
date added to LUP
2016-04-01 15:20:25
date last changed
2021-02-17 02:53:58
@article{6abce049-5161-4773-aba0-ac6fc74c3c1b,
  abstract     = {The gene encoding an alkaline active xylanase of Bacillus halodurans S7, containing an open reading frame of 1188 nucleotides encoding 396 amino acids, was cloned and expressed in Escherchia coli. On the basis of sequence similarity, possible -10 and -35, ribosome binding, and transcription terminator regions were identified. Analysis of the deduced amino acid sequence revealed that the protein was a single domain enyzme belonging to family 10 and designated as xyn10A. The calculated molecular mass and isoelectric point (pI) of the mature peptide were 42.6 and 4.5 kDa, respectively. Xylanase acitivity expressed by the recombinant organism was detected in the cytoplasm, periplasm and the extracellular medium. In an 18-h old culture, about 39% of the xylanase was detected in the medium. The stability and activity profile of the recombinant xylanase was similar to the properties of the enzyme produced by the wild-type organism.},
  author       = {Mamo, Gashaw and Delgado, O and Martinez, A and Mattiasson, Bo and Hatti-Kaul, Rajni},
  issn         = {1559-0305},
  language     = {eng},
  number       = {2},
  pages        = {149--159},
  publisher    = {Humana Press},
  series       = {Molecular Biotechnology},
  title        = {Cloning, sequence analysis, and expression of a gene encoding an endoxylanase from Bacillus halodurans S7},
  volume       = {33},
  year         = {2006},
}