Characterization of AlgMsp, an alginate lyase from Microbulbifer sp. 6532A
Alginate is a polysaccharide produced by certain seaweeds and bacteria that consists of mannuronic acid and guluronic acid residues. Seaweed alginate is used in food and industrial chemical processes, while the biosynthesis of bacterial alginate is associated with pathogenic Pseudomonas aeruginosa....
Gespeichert in:
| Veröffentlicht in: | PloS one 2014-11, Vol.9 (11), p.e112939-e112939 |
|---|---|
| Hauptverfasser: | , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | e112939 |
|---|---|
| container_issue | 11 |
| container_start_page | e112939 |
| container_title | PloS one |
| container_volume | 9 |
| creator | Swift, Steven M Hudgens, Jeffrey W Heselpoth, Ryan D Bales, Patrick M Nelson, Daniel C |
| description | Alginate is a polysaccharide produced by certain seaweeds and bacteria that consists of mannuronic acid and guluronic acid residues. Seaweed alginate is used in food and industrial chemical processes, while the biosynthesis of bacterial alginate is associated with pathogenic Pseudomonas aeruginosa. Alginate lyases cleave this polysaccharide into short oligo-uronates and thus have the potential to be utilized for both industrial and medicinal applications. An alginate lyase gene, algMsp, from Microbulbifer sp. 6532A, was synthesized as an E.coli codon-optimized clone. The resulting 37 kDa recombinant protein, AlgMsp, was expressed, purified and characterized. The alginate lyase displayed highest activity at pH 8 and 0.2 M NaCl. Activity of the alginate lyase was greatest at 50°C; however the enzyme was not stable over time when incubated at 50°C. The alginate lyase was still highly active at 25°C and displayed little or no loss of activity after 24 hours at 25°C. The activity of AlgMsp was not dependent on the presence of divalent cations. Comparing activity of the lyase against polymannuronic acid and polyguluronic acid substrates showed a higher turnover rate for polymannuronic acid. However, AlgMSP exhibited greater catalytic efficiency with the polyguluronic acid substrate. Prolonged AlgMsp-mediated degradation of alginate produced dimer, trimer, tetramer, and pentamer oligo-uronates. |
| doi_str_mv | 10.1371/journal.pone.0112939 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_plos_</sourceid><recordid>TN_cdi_plos_journals_1980721718</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><doaj_id>oai_doaj_org_article_2d51a7de4b69456b89283fa17a1663e8</doaj_id><sourcerecordid>1980721718</sourcerecordid><originalsourceid>FETCH-LOGICAL-c592t-c9945a4783d067b73f8c48080c093c9196f04f9ba166a9127e22f938c3d163fc3</originalsourceid><addsrcrecordid>eNptUk1v1DAQjRAV_YB_gCBSLz2wi-1J_HFBWq2AFrXiAmdr4thbr7xxsBOk9teTZdOqRZw8st9788bziuItJUsKgn7cxjF1GJZ97OySUMoUqBfFCVXAFpwRePmkPi5Oc94SUoPk_FVxzOqKKCrkSfFtfYsJzWCTv8fBx66MrlyFzU3uP5TYlRg2vsPBluEOsy1dirvyxpsUmzE03tlU5n5Z8hrY6nVx5DBk-2Y-z4qfXz7_WF8urr9_vVqvrhemVmxYGKWqGishoSVcNAKcNJUkkhiiwCiquCOVUw1SzlFRJixjToE00FIOzsBZ8f6g24eY9fwNWVMliWBUUDkhrg6INuJW98nvMN3piF7_vYhpozEN3gSrWVtTFK2tGj7Z4o1UTIJDKvbtwe61Ps3dxmZnW2O7IWF4Jvr8pfO3ehN_64qBAOCTwMUskOKv0eZB73w2NgTsbBwn35wJIigRYoKe_wP9_3TVATVtIedk3aMZSvQ-Gg8svY-GnqMx0d49HeSR9JAF-AM2n7SC</addsrcrecordid><sourcetype>Open Website</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1980721718</pqid></control><display><type>article</type><title>Characterization of AlgMsp, an alginate lyase from Microbulbifer sp. 6532A</title><source>MEDLINE</source><source>DOAJ Directory of Open Access Journals</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>PubMed Central</source><source>Free Full-Text Journals in Chemistry</source><source>Public Library of Science (PLoS)</source><creator>Swift, Steven M ; Hudgens, Jeffrey W ; Heselpoth, Ryan D ; Bales, Patrick M ; Nelson, Daniel C</creator><creatorcontrib>Swift, Steven M ; Hudgens, Jeffrey W ; Heselpoth, Ryan D ; Bales, Patrick M ; Nelson, Daniel C</creatorcontrib><description>Alginate is a polysaccharide produced by certain seaweeds and bacteria that consists of mannuronic acid and guluronic acid residues. Seaweed alginate is used in food and industrial chemical processes, while the biosynthesis of bacterial alginate is associated with pathogenic Pseudomonas aeruginosa. Alginate lyases cleave this polysaccharide into short oligo-uronates and thus have the potential to be utilized for both industrial and medicinal applications. An alginate lyase gene, algMsp, from Microbulbifer sp. 6532A, was synthesized as an E.coli codon-optimized clone. The resulting 37 kDa recombinant protein, AlgMsp, was expressed, purified and characterized. The alginate lyase displayed highest activity at pH 8 and 0.2 M NaCl. Activity of the alginate lyase was greatest at 50°C; however the enzyme was not stable over time when incubated at 50°C. The alginate lyase was still highly active at 25°C and displayed little or no loss of activity after 24 hours at 25°C. The activity of AlgMsp was not dependent on the presence of divalent cations. Comparing activity of the lyase against polymannuronic acid and polyguluronic acid substrates showed a higher turnover rate for polymannuronic acid. However, AlgMSP exhibited greater catalytic efficiency with the polyguluronic acid substrate. Prolonged AlgMsp-mediated degradation of alginate produced dimer, trimer, tetramer, and pentamer oligo-uronates.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0112939</identifier><identifier>PMID: 25409178</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Acids ; Algae ; Alginate lyase ; Alginic acid ; Alteromonadaceae - enzymology ; Alteromonadaceae - genetics ; Antibiotics ; Bacteria ; Bacterial Proteins - chemistry ; Bacterial Proteins - genetics ; Biodegradation ; Biofilms ; Biology and Life Sciences ; Biosynthesis ; Biotechnology ; Catalysis ; Cations ; Circular Dichroism ; Cloning ; Divalent cations ; E coli ; Enzyme Stability ; Enzymes ; Escherichia coli - genetics ; Escherichia coli - metabolism ; Food industry ; Food processing ; Genes ; Hexuronic Acids - metabolism ; Mannuronic acid ; pH effects ; Polysaccharide-Lyases - chemistry ; Polysaccharide-Lyases - genetics ; Proteins ; Pseudomonas ; Pseudomonas aeruginosa ; Recombinant Proteins - biosynthesis ; Recombinant Proteins - genetics ; Seaweeds ; Sodium chloride ; Sphingomonas ; Substrate Specificity ; Substrates ; Turnover rate</subject><ispartof>PloS one, 2014-11, Vol.9 (11), p.e112939-e112939</ispartof><rights>2014. This is an open-access article, free of all copyright, and may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose. The work is made available under the Creative Commons CC0 public domain dedication. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2014</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c592t-c9945a4783d067b73f8c48080c093c9196f04f9ba166a9127e22f938c3d163fc3</citedby><cites>FETCH-LOGICAL-c592t-c9945a4783d067b73f8c48080c093c9196f04f9ba166a9127e22f938c3d163fc3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4237336/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4237336/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,2096,2915,23845,27901,27902,53766,53768,79569,79570</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25409178$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Swift, Steven M</creatorcontrib><creatorcontrib>Hudgens, Jeffrey W</creatorcontrib><creatorcontrib>Heselpoth, Ryan D</creatorcontrib><creatorcontrib>Bales, Patrick M</creatorcontrib><creatorcontrib>Nelson, Daniel C</creatorcontrib><title>Characterization of AlgMsp, an alginate lyase from Microbulbifer sp. 6532A</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>Alginate is a polysaccharide produced by certain seaweeds and bacteria that consists of mannuronic acid and guluronic acid residues. Seaweed alginate is used in food and industrial chemical processes, while the biosynthesis of bacterial alginate is associated with pathogenic Pseudomonas aeruginosa. Alginate lyases cleave this polysaccharide into short oligo-uronates and thus have the potential to be utilized for both industrial and medicinal applications. An alginate lyase gene, algMsp, from Microbulbifer sp. 6532A, was synthesized as an E.coli codon-optimized clone. The resulting 37 kDa recombinant protein, AlgMsp, was expressed, purified and characterized. The alginate lyase displayed highest activity at pH 8 and 0.2 M NaCl. Activity of the alginate lyase was greatest at 50°C; however the enzyme was not stable over time when incubated at 50°C. The alginate lyase was still highly active at 25°C and displayed little or no loss of activity after 24 hours at 25°C. The activity of AlgMsp was not dependent on the presence of divalent cations. Comparing activity of the lyase against polymannuronic acid and polyguluronic acid substrates showed a higher turnover rate for polymannuronic acid. However, AlgMSP exhibited greater catalytic efficiency with the polyguluronic acid substrate. Prolonged AlgMsp-mediated degradation of alginate produced dimer, trimer, tetramer, and pentamer oligo-uronates.</description><subject>Acids</subject><subject>Algae</subject><subject>Alginate lyase</subject><subject>Alginic acid</subject><subject>Alteromonadaceae - enzymology</subject><subject>Alteromonadaceae - genetics</subject><subject>Antibiotics</subject><subject>Bacteria</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - genetics</subject><subject>Biodegradation</subject><subject>Biofilms</subject><subject>Biology and Life Sciences</subject><subject>Biosynthesis</subject><subject>Biotechnology</subject><subject>Catalysis</subject><subject>Cations</subject><subject>Circular Dichroism</subject><subject>Cloning</subject><subject>Divalent cations</subject><subject>E coli</subject><subject>Enzyme Stability</subject><subject>Enzymes</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli - metabolism</subject><subject>Food industry</subject><subject>Food processing</subject><subject>Genes</subject><subject>Hexuronic Acids - metabolism</subject><subject>Mannuronic acid</subject><subject>pH effects</subject><subject>Polysaccharide-Lyases - chemistry</subject><subject>Polysaccharide-Lyases - genetics</subject><subject>Proteins</subject><subject>Pseudomonas</subject><subject>Pseudomonas aeruginosa</subject><subject>Recombinant Proteins - biosynthesis</subject><subject>Recombinant Proteins - genetics</subject><subject>Seaweeds</subject><subject>Sodium chloride</subject><subject>Sphingomonas</subject><subject>Substrate Specificity</subject><subject>Substrates</subject><subject>Turnover rate</subject><issn>1932-6203</issn><issn>1932-6203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><sourceid>DOA</sourceid><recordid>eNptUk1v1DAQjRAV_YB_gCBSLz2wi-1J_HFBWq2AFrXiAmdr4thbr7xxsBOk9teTZdOqRZw8st9788bziuItJUsKgn7cxjF1GJZ97OySUMoUqBfFCVXAFpwRePmkPi5Oc94SUoPk_FVxzOqKKCrkSfFtfYsJzWCTv8fBx66MrlyFzU3uP5TYlRg2vsPBluEOsy1dirvyxpsUmzE03tlU5n5Z8hrY6nVx5DBk-2Y-z4qfXz7_WF8urr9_vVqvrhemVmxYGKWqGishoSVcNAKcNJUkkhiiwCiquCOVUw1SzlFRJixjToE00FIOzsBZ8f6g24eY9fwNWVMliWBUUDkhrg6INuJW98nvMN3piF7_vYhpozEN3gSrWVtTFK2tGj7Z4o1UTIJDKvbtwe61Ps3dxmZnW2O7IWF4Jvr8pfO3ehN_64qBAOCTwMUskOKv0eZB73w2NgTsbBwn35wJIigRYoKe_wP9_3TVATVtIedk3aMZSvQ-Gg8svY-GnqMx0d49HeSR9JAF-AM2n7SC</recordid><startdate>20141119</startdate><enddate>20141119</enddate><creator>Swift, Steven M</creator><creator>Hudgens, Jeffrey W</creator><creator>Heselpoth, Ryan D</creator><creator>Bales, Patrick M</creator><creator>Nelson, Daniel C</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QO</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TG</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PDBOC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>20141119</creationdate><title>Characterization of AlgMsp, an alginate lyase from Microbulbifer sp. 6532A</title><author>Swift, Steven M ; Hudgens, Jeffrey W ; Heselpoth, Ryan D ; Bales, Patrick M ; Nelson, Daniel C</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c592t-c9945a4783d067b73f8c48080c093c9196f04f9ba166a9127e22f938c3d163fc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Acids</topic><topic>Algae</topic><topic>Alginate lyase</topic><topic>Alginic acid</topic><topic>Alteromonadaceae - enzymology</topic><topic>Alteromonadaceae - genetics</topic><topic>Antibiotics</topic><topic>Bacteria</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - genetics</topic><topic>Biodegradation</topic><topic>Biofilms</topic><topic>Biology and Life Sciences</topic><topic>Biosynthesis</topic><topic>Biotechnology</topic><topic>Catalysis</topic><topic>Cations</topic><topic>Circular Dichroism</topic><topic>Cloning</topic><topic>Divalent cations</topic><topic>E coli</topic><topic>Enzyme Stability</topic><topic>Enzymes</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli - metabolism</topic><topic>Food industry</topic><topic>Food processing</topic><topic>Genes</topic><topic>Hexuronic Acids - metabolism</topic><topic>Mannuronic acid</topic><topic>pH effects</topic><topic>Polysaccharide-Lyases - chemistry</topic><topic>Polysaccharide-Lyases - genetics</topic><topic>Proteins</topic><topic>Pseudomonas</topic><topic>Pseudomonas aeruginosa</topic><topic>Recombinant Proteins - biosynthesis</topic><topic>Recombinant Proteins - genetics</topic><topic>Seaweeds</topic><topic>Sodium chloride</topic><topic>Sphingomonas</topic><topic>Substrate Specificity</topic><topic>Substrates</topic><topic>Turnover rate</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Swift, Steven M</creatorcontrib><creatorcontrib>Hudgens, Jeffrey W</creatorcontrib><creatorcontrib>Heselpoth, Ryan D</creatorcontrib><creatorcontrib>Bales, Patrick M</creatorcontrib><creatorcontrib>Nelson, Daniel C</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Nursing & Allied Health Database</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Meteorological & Geoastrophysical Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Agricultural Science Collection</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>Advanced Technologies & Aerospace Collection</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Materials Science Database</collection><collection>Nursing & Allied Health Database (Alumni Edition)</collection><collection>Meteorological & Geoastrophysical Abstracts - Academic</collection><collection>ProQuest Engineering Collection</collection><collection>ProQuest Biological Science Collection</collection><collection>Agricultural Science Database</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Engineering Database</collection><collection>Nursing & Allied Health Premium</collection><collection>Advanced Technologies & Aerospace Database</collection><collection>ProQuest Advanced Technologies & Aerospace Collection</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Environmental Science Database</collection><collection>Materials Science Collection</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>Engineering Collection</collection><collection>Environmental Science Collection</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Swift, Steven M</au><au>Hudgens, Jeffrey W</au><au>Heselpoth, Ryan D</au><au>Bales, Patrick M</au><au>Nelson, Daniel C</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of AlgMsp, an alginate lyase from Microbulbifer sp. 6532A</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2014-11-19</date><risdate>2014</risdate><volume>9</volume><issue>11</issue><spage>e112939</spage><epage>e112939</epage><pages>e112939-e112939</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>Alginate is a polysaccharide produced by certain seaweeds and bacteria that consists of mannuronic acid and guluronic acid residues. Seaweed alginate is used in food and industrial chemical processes, while the biosynthesis of bacterial alginate is associated with pathogenic Pseudomonas aeruginosa. Alginate lyases cleave this polysaccharide into short oligo-uronates and thus have the potential to be utilized for both industrial and medicinal applications. An alginate lyase gene, algMsp, from Microbulbifer sp. 6532A, was synthesized as an E.coli codon-optimized clone. The resulting 37 kDa recombinant protein, AlgMsp, was expressed, purified and characterized. The alginate lyase displayed highest activity at pH 8 and 0.2 M NaCl. Activity of the alginate lyase was greatest at 50°C; however the enzyme was not stable over time when incubated at 50°C. The alginate lyase was still highly active at 25°C and displayed little or no loss of activity after 24 hours at 25°C. The activity of AlgMsp was not dependent on the presence of divalent cations. Comparing activity of the lyase against polymannuronic acid and polyguluronic acid substrates showed a higher turnover rate for polymannuronic acid. However, AlgMSP exhibited greater catalytic efficiency with the polyguluronic acid substrate. Prolonged AlgMsp-mediated degradation of alginate produced dimer, trimer, tetramer, and pentamer oligo-uronates.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>25409178</pmid><doi>10.1371/journal.pone.0112939</doi><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1932-6203 |
| ispartof | PloS one, 2014-11, Vol.9 (11), p.e112939-e112939 |
| issn | 1932-6203 1932-6203 |
| language | eng |
| recordid | cdi_plos_journals_1980721718 |
| source | MEDLINE; DOAJ Directory of Open Access Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; Free Full-Text Journals in Chemistry; Public Library of Science (PLoS) |
| subjects | Acids Algae Alginate lyase Alginic acid Alteromonadaceae - enzymology Alteromonadaceae - genetics Antibiotics Bacteria Bacterial Proteins - chemistry Bacterial Proteins - genetics Biodegradation Biofilms Biology and Life Sciences Biosynthesis Biotechnology Catalysis Cations Circular Dichroism Cloning Divalent cations E coli Enzyme Stability Enzymes Escherichia coli - genetics Escherichia coli - metabolism Food industry Food processing Genes Hexuronic Acids - metabolism Mannuronic acid pH effects Polysaccharide-Lyases - chemistry Polysaccharide-Lyases - genetics Proteins Pseudomonas Pseudomonas aeruginosa Recombinant Proteins - biosynthesis Recombinant Proteins - genetics Seaweeds Sodium chloride Sphingomonas Substrate Specificity Substrates Turnover rate |
| title | Characterization of AlgMsp, an alginate lyase from Microbulbifer sp. 6532A |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-13T18%3A49%3A59IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_plos_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Characterization%20of%20AlgMsp,%20an%20alginate%20lyase%20from%20Microbulbifer%20sp.%206532A&rft.jtitle=PloS%20one&rft.au=Swift,%20Steven%20M&rft.date=2014-11-19&rft.volume=9&rft.issue=11&rft.spage=e112939&rft.epage=e112939&rft.pages=e112939-e112939&rft.issn=1932-6203&rft.eissn=1932-6203&rft_id=info:doi/10.1371/journal.pone.0112939&rft_dat=%3Cproquest_plos_%3E1980721718%3C/proquest_plos_%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1980721718&rft_id=info:pmid/25409178&rft_doaj_id=oai_doaj_org_article_2d51a7de4b69456b89283fa17a1663e8&rfr_iscdi=true |