Controlling Carrageenan Structure Using a Novel Formylglycine-Dependent Sulfatase, an Endo-4S-iota-Carrageenan Sulfatase

Carrageenans are sulfated polysaccharides that are found in the cell walls of red algae. These polysaccharides have gelling and texturizing properties that are widely appreciated in industrial applications. However, these functional properties depend strongly on the sulfation of the moieties of the...

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Bibliographic Details
Published in:Marine biotechnology (New York, N.Y.) N.Y.), 2013-06, Vol.15 (3), p.265-274
Main Authors: Préchoux, Aurélie, Genicot, Sabine, Rogniaux, Hélène, Helbert, William
Format: Article
Language:English
Subjects:
Algae
Alteromonas fortis
Aquatic life
Aquatic sciences
Bacterial Proteins - metabolism
Base Sequence
Biomedical and Life Sciences
Biotechnology
Carrageenan - chemistry
Carrageenan - metabolism
Chemical Sciences
Chromatography, High Pressure Liquid
Cloning, Molecular
DNA Primers - genetics
Electrophoresis, Polyacrylamide Gel
Engineering
Enzymes
Freshwater & Marine Ecology
Glycine
Glycoside Hydrolases - metabolism
Life Sciences
Magnetic Resonance Spectroscopy
Marine
Marine biology
Microbiology
Molecular Sequence Data
Molecular Structure
Molecular weight
NMR
Nuclear magnetic resonance
Original Article
Proteins
Pseudoalteromonas - enzymology
Pseudoalteromonas atlantica
Rhodophyta - chemistry
Rosaniline Dyes
Sequence Analysis, DNA
Spectrum analysis
Statistical analysis
Sulfatases - genetics
Sulfatases - metabolism
Sulfates - analysis
Tandem Mass Spectrometry
Zoology
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Summary:Carrageenans are sulfated polysaccharides that are found in the cell walls of red algae. These polysaccharides have gelling and texturizing properties that are widely appreciated in industrial applications. However, these functional properties depend strongly on the sulfation of the moieties of the carrabiose repetition unit. Here we aimed to monitor the sulfate composition of gelling carrageenan. To do so, we screened and purified from Pseudoalteromonas atlantica a 4S-iota carrageenan sulfatase that converts ι-carrabiose into α-carrabiose units. The sequence of this protein matched the annotated Q15XH3 (Uniprot databank) formylglycine-dependent sulfatase found in the P. atlantica genome. With pure enzyme, ι-carrageenan could be transformed into a hybrid ι-/α-carrageenan or pure α-carrageenan. Analysis of the distribution of the carrabiose moieties in hybrid carrageenan chain using enzymatic degradation with Alteromonas fortis ι-carrageenase, coupled with chromatography and NMR spectroscopy experiments, showed that the sulfatase has an endo mode of action. The endo-character and the specificity of the sulfatase made it possible to prepare hybrid κ-/ι-/α-carrageenan and κ-/α-carrageenan starting from κ-/ι-carrageenan.
ISSN:1436-2228
1436-2236
DOI:10.1007/s10126-012-9483-y