Characterization of the biochemical properties of recombinant Xyn10C from a marine bacterium, Saccharophagus degradans 2-40

Ja Kyong Ko, Hyeokjin Ko, Kyoung Heon Kim, In-Geol Choi

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

Endo-1,4-β-xylanases are mostly classified into glycoside hydrolase (GH) family 10 or 11. In this study, we examined the catalytic functions of a recombinant endo-1,4-β-xylanase belonging to GH10 (Xyn10C) from a marine bacterium, Saccharophagus degradans 2-40. Optimal activity of this enzyme was evident at 30 °C and pH 7.0, but activity remained even at low temperatures, indicating its adaptation to cold. With respect to other xylanases known to be active in cold temperatures, Xyn10C is unique in that it showed maximal activity in the presence of 2 M of NaCl. The action patterns of recombinant Xyn10C on xylans from hardwood and softwood differed in part, but the enzyme hydrolyzed polysaccharidic substrates primarily to xylobiose and xylotriose through xylo-oligosaccharides, releasing a small amount of xylose. The Km and Vmax values on birchwood xylan were 10.4 mg mL−1 and 253 µmol mg−1 min−1, respectively. The efficient catalytic function of Xyn10C on short-length xylo-oligosaccharide chains was similar to the typical function of other known GH10 xylanases.

Original languageEnglish
Pages (from-to)1-8
Number of pages8
JournalBioprocess and Biosystems Engineering
DOIs
Publication statusAccepted/In press - 2016 Jan 25

Fingerprint

Xylans
Oligosaccharides
Bacteria
Glycoside Hydrolases
Xylose
Enzymes
Softwoods
Hardwoods
Temperature
Substrates
xylobiose
xylotriose

Keywords

  • Cold-adapted xylanase
  • Endo-1,4-β-xylanohydrolase
  • GH10
  • Saccharophagus degradans 2-40
  • Xyn10C

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering

Cite this

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abstract = "Endo-1,4-β-xylanases are mostly classified into glycoside hydrolase (GH) family 10 or 11. In this study, we examined the catalytic functions of a recombinant endo-1,4-β-xylanase belonging to GH10 (Xyn10C) from a marine bacterium, Saccharophagus degradans 2-40. Optimal activity of this enzyme was evident at 30 °C and pH 7.0, but activity remained even at low temperatures, indicating its adaptation to cold. With respect to other xylanases known to be active in cold temperatures, Xyn10C is unique in that it showed maximal activity in the presence of 2 M of NaCl. The action patterns of recombinant Xyn10C on xylans from hardwood and softwood differed in part, but the enzyme hydrolyzed polysaccharidic substrates primarily to xylobiose and xylotriose through xylo-oligosaccharides, releasing a small amount of xylose. The Km and Vmax values on birchwood xylan were 10.4 mg mL−1 and 253 µmol mg−1 min−1, respectively. The efficient catalytic function of Xyn10C on short-length xylo-oligosaccharide chains was similar to the typical function of other known GH10 xylanases.",
keywords = "Cold-adapted xylanase, Endo-1,4-β-xylanohydrolase, GH10, Saccharophagus degradans 2-40, Xyn10C",
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AU - Kim, Kyoung Heon

AU - Choi, In-Geol

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N2 - Endo-1,4-β-xylanases are mostly classified into glycoside hydrolase (GH) family 10 or 11. In this study, we examined the catalytic functions of a recombinant endo-1,4-β-xylanase belonging to GH10 (Xyn10C) from a marine bacterium, Saccharophagus degradans 2-40. Optimal activity of this enzyme was evident at 30 °C and pH 7.0, but activity remained even at low temperatures, indicating its adaptation to cold. With respect to other xylanases known to be active in cold temperatures, Xyn10C is unique in that it showed maximal activity in the presence of 2 M of NaCl. The action patterns of recombinant Xyn10C on xylans from hardwood and softwood differed in part, but the enzyme hydrolyzed polysaccharidic substrates primarily to xylobiose and xylotriose through xylo-oligosaccharides, releasing a small amount of xylose. The Km and Vmax values on birchwood xylan were 10.4 mg mL−1 and 253 µmol mg−1 min−1, respectively. The efficient catalytic function of Xyn10C on short-length xylo-oligosaccharide chains was similar to the typical function of other known GH10 xylanases.

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