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Sökning: db:Swepub > Mattiasson Bo > (2000-2004) > Hreggvidsson G O

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1.
  • Birgisson, Hakon, et al. (författare)
  • A new thermostable alpha-L-arabinofuranosidase from a novel thermophilic bacterium
  • 2004
  • Ingår i: Biotechnology Letters. - Springer Science. - 0141-5492. ; 26:17, s. 1347-1351
  • Tidskriftsartikel (refereegranskat)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.
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2.
  • Birgisson, Hakon, et al. (författare)
  • Two new thermostable alpha-L-rhamnosidases from a novel thermophilic bacterium
  • 2004
  • Ingår i: Enzyme and Microbial Technology. - Elsevier Inc.. - 0141-0229. ; 34:6, s. 561-571
  • Tidskriftsartikel (refereegranskat)abstract
    • Two new thermostable alpha-L-rhamnosidases with novel substrate hydrolysis pattern were cloned and expressed from a new thermophilic bacterium. Fragments of the two alpha-L-rhamnosidase genes, rhmA and rhmB were identified in a partially sequenced genome of the bacterium. Whole genes were recovered by amplifying flanking sequences with single specific primers and nonspecific walking primers. The recovered Genes were then cloned into Escherichia coli and their enzymes produced and purified. Both enzymes were dimers and the MW of the monomers. were 104 and 107 kDa for RhmA and RhmB, respectively. Both rhamnosidases had a temperature optimum at 70degreesC. RhmA had pH optimum at 7.9 and RhmB had a broad pH optimum of 5.0 to 6.9 and RhmA had over 50% activity in the pH interval 5.0 to 8.7 and RhmB in the pH interval 4.0 to 7.9. Both enzymes had over 20% residual activity after 24-h incubation at 60degreesC. RhmA and RhmB had K values of 0.46 and 0.66 mM and V-max values of 134 and 352 U mg(-1) respectively, on p-nitrophenyl-alpha-L-rhamnopyrano side. Both rhamnosidases were active on both alpha-1,2- and alpha-1,6-linkages to beta-D-glucoside. (C) 2004 Elsevier Inc. All rights reserved.
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  • Resultat 1-2 av 2
Typ av publikation
tidskriftsartikel (2)
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refereegranskat (2)
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Kristjansson, J K (2)
Birgisson, Hakon (2)
Fridjonsson, O (1)
Bahrani-Mougeot, F K (1)
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Fridjonsson, O H (1)
Mort, A (1)
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Lunds universitet (2)
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Engelska (2)
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