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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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Published in: | Marine biotechnology (New York, N.Y.) N.Y.), 2013-06, Vol.15 (3), p.265-274 |
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description | 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. |
doi_str_mv | 10.1007/s10126-012-9483-y |
format | article |
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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.</description><identifier>ISSN: 1436-2228</identifier><identifier>EISSN: 1436-2236</identifier><identifier>DOI: 10.1007/s10126-012-9483-y</identifier><identifier>PMID: 23011004</identifier><language>eng</language><publisher>New York: Springer-Verlag</publisher><subject>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</subject><ispartof>Marine biotechnology (New York, N.Y.), 2013-06, Vol.15 (3), p.265-274</ispartof><rights>Springer Science+Business Media New York 2012</rights><rights>Springer Science+Business Media New York 2013</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c439t-ffdd7859a9743edd42e7fc4f430e865ae9e23e495a09875d877ff0ac9945ad663</citedby><cites>FETCH-LOGICAL-c439t-ffdd7859a9743edd42e7fc4f430e865ae9e23e495a09875d877ff0ac9945ad663</cites><orcidid>0000-0001-6083-2034</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.proquest.com/docview/1327344583/fulltextPDF?pq-origsite=primo$$EPDF$$P50$$Gproquest$$H</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/1327344583?pq-origsite=primo$$EHTML$$P50$$Gproquest$$H</linktohtml><link.rule.ids>230,315,786,790,891,11715,27957,27958,36095,36096,44398,75252</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23011004$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-02108462$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Préchoux, Aurélie</creatorcontrib><creatorcontrib>Genicot, Sabine</creatorcontrib><creatorcontrib>Rogniaux, Hélène</creatorcontrib><creatorcontrib>Helbert, William</creatorcontrib><title>Controlling Carrageenan Structure Using a Novel Formylglycine-Dependent Sulfatase, an Endo-4S-iota-Carrageenan Sulfatase</title><title>Marine biotechnology (New York, N.Y.)</title><addtitle>Mar Biotechnol</addtitle><addtitle>Mar Biotechnol (NY)</addtitle><description>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.</description><subject>Algae</subject><subject>Alteromonas fortis</subject><subject>Aquatic life</subject><subject>Aquatic sciences</subject><subject>Bacterial Proteins - metabolism</subject><subject>Base Sequence</subject><subject>Biomedical and Life Sciences</subject><subject>Biotechnology</subject><subject>Carrageenan - chemistry</subject><subject>Carrageenan - metabolism</subject><subject>Chemical Sciences</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Cloning, Molecular</subject><subject>DNA Primers - genetics</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Engineering</subject><subject>Enzymes</subject><subject>Freshwater & Marine Ecology</subject><subject>Glycine</subject><subject>Glycoside Hydrolases - metabolism</subject><subject>Life 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N.Y.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Préchoux, Aurélie</au><au>Genicot, Sabine</au><au>Rogniaux, Hélène</au><au>Helbert, William</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Controlling Carrageenan Structure Using a Novel Formylglycine-Dependent Sulfatase, an Endo-4S-iota-Carrageenan Sulfatase</atitle><jtitle>Marine biotechnology (New York, N.Y.)</jtitle><stitle>Mar Biotechnol</stitle><addtitle>Mar Biotechnol (NY)</addtitle><date>2013-06-01</date><risdate>2013</risdate><volume>15</volume><issue>3</issue><spage>265</spage><epage>274</epage><pages>265-274</pages><issn>1436-2228</issn><eissn>1436-2236</eissn><notes>ObjectType-Article-1</notes><notes>SourceType-Scholarly Journals-1</notes><notes>ObjectType-Feature-2</notes><notes>content type line 23</notes><abstract>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.</abstract><cop>New York</cop><pub>Springer-Verlag</pub><pmid>23011004</pmid><doi>10.1007/s10126-012-9483-y</doi><tpages>10</tpages><orcidid>https://orcid.org/0000-0001-6083-2034</orcidid></addata></record> |
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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 |
title | Controlling Carrageenan Structure Using a Novel Formylglycine-Dependent Sulfatase, an Endo-4S-iota-Carrageenan Sulfatase |
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