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Enzyme-Assisted Preparation of Furcellaran-Like κ-/β-Carrageenan

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Abstract

Carrageenans are sulfated galactans that are widely used in industrial applications for their thickening and gelling properties, which vary according to the amount and distribution of ester sulfate groups along the galactan backbone. To determine and direct the sulfation of κ-carrageenan moieties, we purified an endo-κ-carrageenan sulfatase (Q15XH1 accession in UniprotKB) from Pseudoalteromonas atlantica T6c extracts. Based on sequence analyses and exploration of the genomic environment of Q15XH1, we discovered and characterized a second endo-κ-carrageenan sulfatase (Q15XG7 accession in UniprotKB). Both enzymes convert κ-carrageenan into a hybrid, furcellaran-like κ-/β-carrageenan. We compared the protein sequences of these two new κ-carrageenan sulfatases and that of a previously reported ι-carrageenan sulfatase with other predicted sulfatases in the P. atlantica genome, revealing the existence of additional new carrageenan sulfatases.

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Acknowledgments

The research leading to these results received funding from the European Community Seventh Framework Programme (FP7) under grant agreement no. 222628. Mass spectrometry analyses were conducted at the BIBS facility at the INRA Biopolymers Interaction Assemblies research unit (www.bibs.inra.fr). We thank Mathilde Joint for her excellent technical assistance in LC-MS/MS. Special thanks to Nelly Kervarec from the “University of Bretagne Occidentale” for her expertise in the NMR analyses.

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Authors and Affiliations

  1. Sorbonne Universités, UPMC Univ Paris 06, UMR 8227, Integrative Biology of Marine Models, Station Biologique de Roscoff, 29680, Roscoff, France

    Aurélie Préchoux, Sabine Genicot & William Helbert

  2. CNRS, UMR 8227, Integrative Biology of Marine Models, Station Biologique de Roscoff, 29680, Roscoff, France

    Aurélie Préchoux, Sabine Genicot & William Helbert

  3. INRA, Biopolymers Interactions Assemblies, 44316, Nantes, France

    Hélène Rogniaux

  4. Centre de Recherches sur les Macromolécules Végétales (CERMAV, UPR-CNRS 5301), Affiliated with the Université Joseph Fourier (UJF), BP53, 38041, Grenoble Cedex 9, France

    William Helbert

  5. Institut de Chimie Moléculaire de Grenoble (ICMG, FR-CNRS 2607), Grenoble Cedex 9, France

    William Helbert

Authors
  1. Aurélie Préchoux
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  2. Sabine Genicot
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  3. Hélène Rogniaux
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  4. William Helbert
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Corresponding author

Correspondence to William Helbert.

Electronic Supplementary Material

Structural alignment of proteins annotated as sulfatases in P. atlantica T6c and other bacterial and human sulfatases that have been biochemically and structurally characterized. The alignment calculated with T-Coffee in mode Expresso (Notredame et al. 2000) is presented with ESPript (Robert and Gouet 2014). Conserved amino acids and highly conserved amino acids are underlined in red and yellow, respectively. Alpha-helices and beta-strands are shown as helices (α1 to α15) and arrows (β1 to β18), respectively, and beta-turns are indicated by TT.

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Préchoux, A., Genicot, S., Rogniaux, H. et al. Enzyme-Assisted Preparation of Furcellaran-Like κ-/β-Carrageenan. Mar Biotechnol 18, 133–143 (2016). https://doi.org/10.1007/s10126-015-9675-3

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  • DOI: https://doi.org/10.1007/s10126-015-9675-3

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