Cloning, sequence analysis, and expression of a gene encoding an endoxylanase from Bacillus halodurans S7
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/407368
- author
- Mamo, Gashaw LU ; Delgado, O ; Martinez, A ; Mattiasson, Bo LU and Hatti-Kaul, Rajni LU
- organization
- publishing date
- 2006
- 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
- 2022-01-28 04:54:08
@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}},
keywords = {{purification; expression; alkaliphile; endoxylanase; Bacillus halodurans}},
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}},
}