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A new thermostable alpha-L-arabinofuranosidase from a novel thermophilic bacterium

Birgisson, Hakon LU ; Fridjonsson, O; Bahrani-Mougeot, F K; Hreggvidsson, G O; Kristjansson, J K and Mattiasson, Bo LU (2004) In Biotechnology Letters 26(17). p.1347-1351
Abstract
An alpha-L-arabinofuranosidase gene was identified in a sequenced genome of a novel thermophilic bacterium, which belongs to the recently described phylum of Thermomicrobia. Amino acid sequence comparison of the enzyme (designated AraF) revealed similarity to glycoside hydrolases of family 51. The gene was cloned into Escherichia coli and its recombinant product expressed and purified. The enzyme appeared to be a hexamer. AraF was optimally active at 70degreesC (over 10 min) and pH 6 having 92% residual activity after 1 h at 70degreesC. AraF had a K-m value of 0.6 rum and V-max value of 122 U mg(-1) on p-nitrophenyl-alpha-L-arabinofuranoside. AraF was almost equally active on branched arabinan and debranched arabinan, properties not... (More)
An alpha-L-arabinofuranosidase gene was identified in a sequenced genome of a novel thermophilic bacterium, which belongs to the recently described phylum of Thermomicrobia. Amino acid sequence comparison of the enzyme (designated AraF) revealed similarity to glycoside hydrolases of family 51. The gene was cloned into Escherichia coli and its recombinant product expressed and purified. The enzyme appeared to be a hexamer. AraF was optimally active at 70degreesC (over 10 min) and pH 6 having 92% residual activity after 1 h at 70degreesC. AraF had a K-m value of 0.6 rum and V-max value of 122 U mg(-1) on p-nitrophenyl-alpha-L-arabinofuranoside. AraF was almost equally active on branched arabinan and debranched arabinan, properties not previously found in alpha-L-arabinofuranosidases in GH family 51. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Biotechnology Letters
volume
26
issue
17
pages
1347 - 1351
publisher
Springer
external identifiers
  • wos:000225103700006
  • pmid:15604762
  • scopus:21644450112
ISSN
1573-6776
DOI
10.1023/B:BILE.0000045631.57073.79
language
English
LU publication?
yes
id
22171701-e24d-4a5f-a9ff-ea146c72b7c2 (old id 140528)
date added to LUP
2007-07-02 08:07:36
date last changed
2017-10-22 04:34:28
@article{22171701-e24d-4a5f-a9ff-ea146c72b7c2,
  abstract     = {An alpha-L-arabinofuranosidase gene was identified in a sequenced genome of a novel thermophilic bacterium, which belongs to the recently described phylum of Thermomicrobia. Amino acid sequence comparison of the enzyme (designated AraF) revealed similarity to glycoside hydrolases of family 51. The gene was cloned into Escherichia coli and its recombinant product expressed and purified. The enzyme appeared to be a hexamer. AraF was optimally active at 70degreesC (over 10 min) and pH 6 having 92% residual activity after 1 h at 70degreesC. AraF had a K-m value of 0.6 rum and V-max value of 122 U mg(-1) on p-nitrophenyl-alpha-L-arabinofuranoside. AraF was almost equally active on branched arabinan and debranched arabinan, properties not previously found in alpha-L-arabinofuranosidases in GH family 51.},
  author       = {Birgisson, Hakon and Fridjonsson, O and Bahrani-Mougeot, F K and Hreggvidsson, G O and Kristjansson, J K and Mattiasson, Bo},
  issn         = {1573-6776},
  language     = {eng},
  number       = {17},
  pages        = {1347--1351},
  publisher    = {Springer},
  series       = {Biotechnology Letters},
  title        = {A new thermostable alpha-L-arabinofuranosidase from a novel thermophilic bacterium},
  url          = {http://dx.doi.org/10.1023/B:BILE.0000045631.57073.79},
  volume       = {26},
  year         = {2004},
}