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Characterisation of a phylogenetically distinct PL25 family ulvan lyase from a seaweed biomass enriched metagenome

Jasilionis, Andrius LU ; Sivakumar, Pavithra ; Dobruchowska, Justyna M. ; Fjermedal, Sune ; Guðmundsson, Hörður ; Adalsteinsson, Bjorn Thor ; Hreggviðsson, Guðmundur Ó. ; Meyer, Anne S. and Nordberg Karlsson, Eva LU orcid (2026) In The FEBS Journal
Abstract
Ulvan is a polysaccharide most abundant in green macroalgae biomass.
Investigation of ulvan confirmed the potential of the polysaccharide for
food, pharmaceutical and chemistry applications, emphasising the
beneficial properties of ulvan oligosaccharides. Efficient production of
oligosaccharides requires action of ulvan lyases capable of ensuring
polysaccharide enzymatic depolymerisation. The armoury of available
ulvan lyases was expanded by characterisation of SH2L_Ulv3 ulvan lyase,
which was found to be phylogenetically distinct from previously
characterised lyases attributed to PL25 family. A gene encoding a novel
ulvan lyase was identified among sequences from a seaweed biomass
... (More)
Ulvan is a polysaccharide most abundant in green macroalgae biomass.
Investigation of ulvan confirmed the potential of the polysaccharide for
food, pharmaceutical and chemistry applications, emphasising the
beneficial properties of ulvan oligosaccharides. Efficient production of
oligosaccharides requires action of ulvan lyases capable of ensuring
polysaccharide enzymatic depolymerisation. The armoury of available
ulvan lyases was expanded by characterisation of SH2L_Ulv3 ulvan lyase,
which was found to be phylogenetically distinct from previously
characterised lyases attributed to PL25 family. A gene encoding a novel
ulvan lyase was identified among sequences from a seaweed biomass
metagenome enriched in an intertidal coastal hot spring. Identified
ulvan lyase was most similar to a hypothetical protein from a
Bacteroidales bacterium. Recombinant SH2L_Ulv3 was heterologously
(over)produced in Escherichia coli at a high yield, remaining
soluble in the expression host as well as after affinity purification.
Ulvan lyase active as a 48.6 kDa monomer with evaluated activity optimum
pH 7.5 and 200 mm NaCl at 25 °C
demonstrated broad substrate specificity. SH2L_Ulv3 degraded ulvan from
blade-thallus as well as tubular-thallus morphology algae species,
efficiently producing three different DP4 and DP2 unsaturated
oligosaccharides. The kinetic parameters of SH2L_Ulv3 were KM 3.63 ± 0.12 mg·mL−1, Vmax 1.78 ± 0.04 μmol·min−1·mL−1 and kcat 1.46 ± 0.04 s−1. Magnesium ion stimulated SH2L_Ulv3 activity. The characterised enzyme was not thermostable, displaying Tm
42 °C. The computationally modelled structure of SH2L_Ulv3 revealed
structural organisation and active site architecture as well as ligand
substrate binding and zinc ion coordinating residues typical for PL25
lyases; however, with a larger central active site cleft facilitating
ulvan polysaccharide degradation. (Less)
Please use this url to cite or link to this publication:
author
; ; ; ; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
epub
subject
keywords
Ulvan lyase
in
The FEBS Journal
publisher
John Wiley & Sons Inc.
external identifiers
  • scopus:105028119226
  • pmid:41562434
ISSN
1742-464X
DOI
10.1111/febs.70390
language
English
LU publication?
yes
additional info
© 2026 The Author(s). The FEBS Journal published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.
id
17267610-5f07-43b1-99bb-299a0c054ffc
date added to LUP
2026-02-08 20:03:28
date last changed
2026-02-10 03:16:51
@article{17267610-5f07-43b1-99bb-299a0c054ffc,
  abstract     = {{Ulvan is a polysaccharide most abundant in green macroalgae biomass. <br>
Investigation of ulvan confirmed the potential of the polysaccharide for<br>
 food, pharmaceutical and chemistry applications, emphasising the <br>
beneficial properties of ulvan oligosaccharides. Efficient production of<br>
 oligosaccharides requires action of ulvan lyases capable of ensuring <br>
polysaccharide enzymatic depolymerisation. The armoury of available <br>
ulvan lyases was expanded by characterisation of SH2L_Ulv3 ulvan lyase, <br>
which was found to be phylogenetically distinct from previously <br>
characterised lyases attributed to PL25 family. A gene encoding a novel <br>
ulvan lyase was identified among sequences from a seaweed biomass <br>
metagenome enriched in an intertidal coastal hot spring. Identified <br>
ulvan lyase was most similar to a hypothetical protein from a <br>
Bacteroidales bacterium. Recombinant SH2L_Ulv3 was heterologously <br>
(over)produced in <i>Escherichia coli</i> at a high yield, remaining <br>
soluble in the expression host as well as after affinity purification. <br>
Ulvan lyase active as a 48.6 kDa monomer with evaluated activity optimum<br>
 pH 7.5 and 200 mm NaCl at 25 °C <br>
demonstrated broad substrate specificity. SH2L_Ulv3 degraded ulvan from <br>
blade-thallus as well as tubular-thallus morphology algae species, <br>
efficiently producing three different DP4 and DP2 unsaturated <br>
oligosaccharides. The kinetic parameters of SH2L_Ulv3 were <i>K</i><sub>M</sub> 3.63 ± 0.12 mg·mL<sup>−1</sup>, <i>V</i><sub>max</sub> 1.78 ± 0.04 μmol·min<sup>−1</sup>·mL<sup>−1</sup> and <i>k</i><sub>cat</sub> 1.46 ± 0.04 s<sup>−1</sup>. Magnesium ion stimulated SH2L_Ulv3 activity. The characterised enzyme was not thermostable, displaying <i>T</i><sub>m</sub><br>
 42 °C. The computationally modelled structure of SH2L_Ulv3 revealed <br>
structural organisation and active site architecture as well as ligand <br>
substrate binding and zinc ion coordinating residues typical for PL25 <br>
lyases; however, with a larger central active site cleft facilitating <br>
ulvan polysaccharide degradation.}},
  author       = {{Jasilionis, Andrius and Sivakumar, Pavithra and Dobruchowska, Justyna M. and Fjermedal, Sune and Guðmundsson, Hörður and Adalsteinsson, Bjorn Thor and Hreggviðsson, Guðmundur Ó. and Meyer, Anne S. and Nordberg Karlsson, Eva}},
  issn         = {{1742-464X}},
  keywords     = {{Ulvan lyase}},
  language     = {{eng}},
  month        = {{01}},
  publisher    = {{John Wiley & Sons Inc.}},
  series       = {{The FEBS Journal}},
  title        = {{Characterisation of a phylogenetically distinct PL25 family ulvan lyase from a seaweed biomass enriched metagenome}},
  url          = {{http://dx.doi.org/10.1111/febs.70390}},
  doi          = {{10.1111/febs.70390}},
  year         = {{2026}},
}