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Enzymatic specificity and hydrolysis pattern of the catalytic domain of the xylanase Xyn1 from Rhodothermus marinus

Karlsson, Eva Nordberg LU orcid ; Dahlberg, Leif LU ; Torto, Nelson LU ; Gorton, Lo LU and Holst, Olle LU (1998) In Journal of Biotechnology 60(1-2). p.23-25
Abstract

The catalytic domain of a xylanase from Rhodothermus marinus was produced in Escherichia coli. The catalytic domain belongs to glycosyl hydrolase family 10. The produced protein has a 22-amino acid leader peptide followed by a 411-amino acid truncated xylanase. The molecular mass was 48 kDa and the recombinant xylanase had a pI of 4.9. The pH and temperature optima for activity were determined to be 7.5 and 80°C, respectively. At that temperature the enzyme had a half-life of 1 h 40 min. An addition of 1 mM calcium stabilized the activity of the enzyme at 80°C. The xylanase had its highest specific activity on oat spelt xylan but was active also on other xylans and to a limited extent on some other polysaccharides (soluble glucans). No... (More)

The catalytic domain of a xylanase from Rhodothermus marinus was produced in Escherichia coli. The catalytic domain belongs to glycosyl hydrolase family 10. The produced protein has a 22-amino acid leader peptide followed by a 411-amino acid truncated xylanase. The molecular mass was 48 kDa and the recombinant xylanase had a pI of 4.9. The pH and temperature optima for activity were determined to be 7.5 and 80°C, respectively. At that temperature the enzyme had a half-life of 1 h 40 min. An addition of 1 mM calcium stabilized the activity of the enzyme at 80°C. The xylanase had its highest specific activity on oat spelt xylan but was active also on other xylans and to a limited extent on some other polysaccharides (soluble glucans). No exo- or endo-cellulase activity was observed. Hydrolysis of xylo-oligomers and oat spelt xylan was studied and the predominant products of hydrolysis were xylobiose and xylotriose. The enzyme was inactive on xylobiose, xylotriose and on the soluble fraction from oat spelt xylan. The R. marinus xylanase is shown to have a strong preference for internal linkages and is therefore classified as an endo-xylanase. Copyright (C) 1998 Elsevier Science B.V.

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author
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organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Glycosyl hydrolase family 10, Rhodothermus marinus, Xylanase
in
Journal of Biotechnology
volume
60
issue
1-2
pages
3 pages
publisher
Elsevier
external identifiers
  • scopus:0038687875
  • pmid:9571799
ISSN
0168-1656
DOI
10.1016/S0168-1656(97)00178-8
language
English
LU publication?
yes
id
c0e3dda7-b78f-4f4e-9eb6-14676f69ec5d
date added to LUP
2018-11-14 21:15:32
date last changed
2024-05-13 19:46:49
@article{c0e3dda7-b78f-4f4e-9eb6-14676f69ec5d,
  abstract     = {{<p>The catalytic domain of a xylanase from Rhodothermus marinus was produced in Escherichia coli. The catalytic domain belongs to glycosyl hydrolase family 10. The produced protein has a 22-amino acid leader peptide followed by a 411-amino acid truncated xylanase. The molecular mass was 48 kDa and the recombinant xylanase had a pI of 4.9. The pH and temperature optima for activity were determined to be 7.5 and 80°C, respectively. At that temperature the enzyme had a half-life of 1 h 40 min. An addition of 1 mM calcium stabilized the activity of the enzyme at 80°C. The xylanase had its highest specific activity on oat spelt xylan but was active also on other xylans and to a limited extent on some other polysaccharides (soluble glucans). No exo- or endo-cellulase activity was observed. Hydrolysis of xylo-oligomers and oat spelt xylan was studied and the predominant products of hydrolysis were xylobiose and xylotriose. The enzyme was inactive on xylobiose, xylotriose and on the soluble fraction from oat spelt xylan. The R. marinus xylanase is shown to have a strong preference for internal linkages and is therefore classified as an endo-xylanase. Copyright (C) 1998 Elsevier Science B.V.</p>}},
  author       = {{Karlsson, Eva Nordberg and Dahlberg, Leif and Torto, Nelson and Gorton, Lo and Holst, Olle}},
  issn         = {{0168-1656}},
  keywords     = {{Glycosyl hydrolase family 10; Rhodothermus marinus; Xylanase}},
  language     = {{eng}},
  month        = {{02}},
  number       = {{1-2}},
  pages        = {{23--25}},
  publisher    = {{Elsevier}},
  series       = {{Journal of Biotechnology}},
  title        = {{Enzymatic specificity and hydrolysis pattern of the catalytic domain of the xylanase Xyn1 from Rhodothermus marinus}},
  url          = {{http://dx.doi.org/10.1016/S0168-1656(97)00178-8}},
  doi          = {{10.1016/S0168-1656(97)00178-8}},
  volume       = {{60}},
  year         = {{1998}},
}