Characterization of an extracellular biofunctional alginate lyase from marine Microbulbifer sp. ALW1 and antioxidant activity of enzymatic hydrolysates
A novel alginate-degrading marine bacterium Microbulbifer sp. ALW1 was isolated from rotten brown alga. An extracellular alginate lyase was purified to electrophoretic homogeneity and had a molecular mass of about 26.0kDa determined by SDS-PAGE and size exclusion chromatography. This enzyme showed a...
Gespeichert in:
| Veröffentlicht in: | Microbiological research 2016-01, Vol.182, p.49-58 |
|---|---|
| Hauptverfasser: | , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 58 |
|---|---|
| container_issue | |
| container_start_page | 49 |
| container_title | Microbiological research |
| container_volume | 182 |
| creator | Zhu, Yanbing Wu, Liyun Chen, Yanhong Ni, Hui Xiao, Anfeng Cai, Huinong |
| description | A novel alginate-degrading marine bacterium Microbulbifer sp. ALW1 was isolated from rotten brown alga. An extracellular alginate lyase was purified to electrophoretic homogeneity and had a molecular mass of about 26.0kDa determined by SDS-PAGE and size exclusion chromatography. This enzyme showed activities towards both polyguluronate and polymannuronate indicating its bifunctionality while with preference for the former substrate. Using sodium alginate as a substrate, strain ALW1 alginate lyase was optimally active at 45°C and pH 7.0. It was stable at 25°C, 30°C, 35°C and 40°C, but not stable at 50°C. This alginate lyase showed good stability over a broad pH range (5.0–9.0). The enzyme activity was increased to 5.1 times by adding NaCl to a final concentration of 0.5M. Strain ALW1 alginate lyase produced disaccharide (majority) and trisaccharide from alginate indicating that this enzyme could be a good tool for preparation of alginate oligosaccharides with low degree of polymerization (DP). The alginate oligosaccharides displayed the scavenging abilities towards radicals (DPPH, ABTS+ and hydroxyl) and the reducing power. Therefore, the hydrolysates exhibited the antioxidant activity and had potential as a natural antioxidant. |
| doi_str_mv | 10.1016/j.micres.2015.09.004 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_1805510776</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0944501315300082</els_id><sourcerecordid>1751195503</sourcerecordid><originalsourceid>FETCH-LOGICAL-c441t-4a1db874138ebd32116548874bcee2df57c196938f123248587dffe3943957a53</originalsourceid><addsrcrecordid>eNqFUctu1DAUjRCIDoU_QMhLNgm-8SPOBqkaQYs0iA2IpeXY19SjPAY7qZr-CL-LoyksYWFd6fo87HOK4jXQCijId8dqCDZiqmoKoqJtRSl_UuxAgiqprNnTYkdbzktBgV0UL1I6Ugq8VfXz4qKWUkkJbFf82t-aaOyMMTyYOUwjmTwxI8H7Oa-x75feRNKFyS-j3e5NT0z_I4xmRtKvJiHxcRrIYGIYkXzOT5q6pe-Cx0jSqSJXh--QBV0-mX4fXJ4kG4a7MK-bGY4P65CtLbldXZz6NWXp9LJ45k2f8NXjvCy-ffzwdX9THr5cf9pfHUrLOcwlN-A61XBgCjvHagApuMqLziLWzovGQitbpjzUrOZKqMZ5j6zlrBWNEeyyeHvWPcXp54Jp1kNI27_NiNOSNCgqBNCmkf-HNgKgFYKyDOVnaE4jpYhen2LIEa0aqN7a00d9bk9v7Wna6txepr15dFi6Ad1f0p-6MuD9GYA5kruAUScbcLToQkQ7azeFfzv8Bh3Ur78</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1751195503</pqid></control><display><type>article</type><title>Characterization of an extracellular biofunctional alginate lyase from marine Microbulbifer sp. ALW1 and antioxidant activity of enzymatic hydrolysates</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals</source><source>EZB-FREE-00999 freely available EZB journals</source><creator>Zhu, Yanbing ; Wu, Liyun ; Chen, Yanhong ; Ni, Hui ; Xiao, Anfeng ; Cai, Huinong</creator><creatorcontrib>Zhu, Yanbing ; Wu, Liyun ; Chen, Yanhong ; Ni, Hui ; Xiao, Anfeng ; Cai, Huinong</creatorcontrib><description>A novel alginate-degrading marine bacterium Microbulbifer sp. ALW1 was isolated from rotten brown alga. An extracellular alginate lyase was purified to electrophoretic homogeneity and had a molecular mass of about 26.0kDa determined by SDS-PAGE and size exclusion chromatography. This enzyme showed activities towards both polyguluronate and polymannuronate indicating its bifunctionality while with preference for the former substrate. Using sodium alginate as a substrate, strain ALW1 alginate lyase was optimally active at 45°C and pH 7.0. It was stable at 25°C, 30°C, 35°C and 40°C, but not stable at 50°C. This alginate lyase showed good stability over a broad pH range (5.0–9.0). The enzyme activity was increased to 5.1 times by adding NaCl to a final concentration of 0.5M. Strain ALW1 alginate lyase produced disaccharide (majority) and trisaccharide from alginate indicating that this enzyme could be a good tool for preparation of alginate oligosaccharides with low degree of polymerization (DP). The alginate oligosaccharides displayed the scavenging abilities towards radicals (DPPH, ABTS+ and hydroxyl) and the reducing power. Therefore, the hydrolysates exhibited the antioxidant activity and had potential as a natural antioxidant.</description><identifier>ISSN: 0944-5013</identifier><identifier>EISSN: 1618-0623</identifier><identifier>DOI: 10.1016/j.micres.2015.09.004</identifier><identifier>PMID: 26686613</identifier><language>eng</language><publisher>Germany: Elsevier GmbH</publisher><subject>Alginate lyase ; Alginate oligosaccharides ; Alginates - metabolism ; Antioxidant activity ; Antioxidants - chemistry ; Antioxidants - metabolism ; Bacterial Proteins - chemistry ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Characterization ; Enzyme Stability ; Gammaproteobacteria - classification ; Gammaproteobacteria - enzymology ; Gammaproteobacteria - genetics ; Gammaproteobacteria - isolation & purification ; Glucuronic Acid - metabolism ; Hexuronic Acids - metabolism ; Hydrogen-Ion Concentration ; Microbulbifer sp ; Molecular Sequence Data ; Molecular Weight ; Phylogeny ; Polysaccharide-Lyases - chemistry ; Polysaccharide-Lyases - genetics ; Polysaccharide-Lyases - metabolism ; Seawater - microbiology ; Substrate Specificity ; Temperature</subject><ispartof>Microbiological research, 2016-01, Vol.182, p.49-58</ispartof><rights>2015 Elsevier GmbH</rights><rights>Copyright © 2015 Elsevier GmbH. All rights reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c441t-4a1db874138ebd32116548874bcee2df57c196938f123248587dffe3943957a53</citedby><cites>FETCH-LOGICAL-c441t-4a1db874138ebd32116548874bcee2df57c196938f123248587dffe3943957a53</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0944501315300082$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26686613$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zhu, Yanbing</creatorcontrib><creatorcontrib>Wu, Liyun</creatorcontrib><creatorcontrib>Chen, Yanhong</creatorcontrib><creatorcontrib>Ni, Hui</creatorcontrib><creatorcontrib>Xiao, Anfeng</creatorcontrib><creatorcontrib>Cai, Huinong</creatorcontrib><title>Characterization of an extracellular biofunctional alginate lyase from marine Microbulbifer sp. ALW1 and antioxidant activity of enzymatic hydrolysates</title><title>Microbiological research</title><addtitle>Microbiol Res</addtitle><description>A novel alginate-degrading marine bacterium Microbulbifer sp. ALW1 was isolated from rotten brown alga. An extracellular alginate lyase was purified to electrophoretic homogeneity and had a molecular mass of about 26.0kDa determined by SDS-PAGE and size exclusion chromatography. This enzyme showed activities towards both polyguluronate and polymannuronate indicating its bifunctionality while with preference for the former substrate. Using sodium alginate as a substrate, strain ALW1 alginate lyase was optimally active at 45°C and pH 7.0. It was stable at 25°C, 30°C, 35°C and 40°C, but not stable at 50°C. This alginate lyase showed good stability over a broad pH range (5.0–9.0). The enzyme activity was increased to 5.1 times by adding NaCl to a final concentration of 0.5M. Strain ALW1 alginate lyase produced disaccharide (majority) and trisaccharide from alginate indicating that this enzyme could be a good tool for preparation of alginate oligosaccharides with low degree of polymerization (DP). The alginate oligosaccharides displayed the scavenging abilities towards radicals (DPPH, ABTS+ and hydroxyl) and the reducing power. Therefore, the hydrolysates exhibited the antioxidant activity and had potential as a natural antioxidant.</description><subject>Alginate lyase</subject><subject>Alginate oligosaccharides</subject><subject>Alginates - metabolism</subject><subject>Antioxidant activity</subject><subject>Antioxidants - chemistry</subject><subject>Antioxidants - metabolism</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>Characterization</subject><subject>Enzyme Stability</subject><subject>Gammaproteobacteria - classification</subject><subject>Gammaproteobacteria - enzymology</subject><subject>Gammaproteobacteria - genetics</subject><subject>Gammaproteobacteria - isolation & purification</subject><subject>Glucuronic Acid - metabolism</subject><subject>Hexuronic Acids - metabolism</subject><subject>Hydrogen-Ion Concentration</subject><subject>Microbulbifer sp</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>Phylogeny</subject><subject>Polysaccharide-Lyases - chemistry</subject><subject>Polysaccharide-Lyases - genetics</subject><subject>Polysaccharide-Lyases - metabolism</subject><subject>Seawater - microbiology</subject><subject>Substrate Specificity</subject><subject>Temperature</subject><issn>0944-5013</issn><issn>1618-0623</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFUctu1DAUjRCIDoU_QMhLNgm-8SPOBqkaQYs0iA2IpeXY19SjPAY7qZr-CL-LoyksYWFd6fo87HOK4jXQCijId8dqCDZiqmoKoqJtRSl_UuxAgiqprNnTYkdbzktBgV0UL1I6Ugq8VfXz4qKWUkkJbFf82t-aaOyMMTyYOUwjmTwxI8H7Oa-x75feRNKFyS-j3e5NT0z_I4xmRtKvJiHxcRrIYGIYkXzOT5q6pe-Cx0jSqSJXh--QBV0-mX4fXJ4kG4a7MK-bGY4P65CtLbldXZz6NWXp9LJ45k2f8NXjvCy-ffzwdX9THr5cf9pfHUrLOcwlN-A61XBgCjvHagApuMqLziLWzovGQitbpjzUrOZKqMZ5j6zlrBWNEeyyeHvWPcXp54Jp1kNI27_NiNOSNCgqBNCmkf-HNgKgFYKyDOVnaE4jpYhen2LIEa0aqN7a00d9bk9v7Wna6txepr15dFi6Ad1f0p-6MuD9GYA5kruAUScbcLToQkQ7azeFfzv8Bh3Ur78</recordid><startdate>201601</startdate><enddate>201601</enddate><creator>Zhu, Yanbing</creator><creator>Wu, Liyun</creator><creator>Chen, Yanhong</creator><creator>Ni, Hui</creator><creator>Xiao, Anfeng</creator><creator>Cai, Huinong</creator><general>Elsevier GmbH</general><scope>6I.</scope><scope>AAFTH</scope><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>7X8</scope><scope>7TN</scope><scope>F1W</scope><scope>H95</scope><scope>L.G</scope></search><sort><creationdate>201601</creationdate><title>Characterization of an extracellular biofunctional alginate lyase from marine Microbulbifer sp. ALW1 and antioxidant activity of enzymatic hydrolysates</title><author>Zhu, Yanbing ; Wu, Liyun ; Chen, Yanhong ; Ni, Hui ; Xiao, Anfeng ; Cai, Huinong</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c441t-4a1db874138ebd32116548874bcee2df57c196938f123248587dffe3943957a53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Alginate lyase</topic><topic>Alginate oligosaccharides</topic><topic>Alginates - metabolism</topic><topic>Antioxidant activity</topic><topic>Antioxidants - chemistry</topic><topic>Antioxidants - metabolism</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - metabolism</topic><topic>Characterization</topic><topic>Enzyme Stability</topic><topic>Gammaproteobacteria - classification</topic><topic>Gammaproteobacteria - enzymology</topic><topic>Gammaproteobacteria - genetics</topic><topic>Gammaproteobacteria - isolation & purification</topic><topic>Glucuronic Acid - metabolism</topic><topic>Hexuronic Acids - metabolism</topic><topic>Hydrogen-Ion Concentration</topic><topic>Microbulbifer sp</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>Phylogeny</topic><topic>Polysaccharide-Lyases - chemistry</topic><topic>Polysaccharide-Lyases - genetics</topic><topic>Polysaccharide-Lyases - metabolism</topic><topic>Seawater - microbiology</topic><topic>Substrate Specificity</topic><topic>Temperature</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zhu, Yanbing</creatorcontrib><creatorcontrib>Wu, Liyun</creatorcontrib><creatorcontrib>Chen, Yanhong</creatorcontrib><creatorcontrib>Ni, Hui</creatorcontrib><creatorcontrib>Xiao, Anfeng</creatorcontrib><creatorcontrib>Cai, Huinong</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>Oceanic Abstracts</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><jtitle>Microbiological research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zhu, Yanbing</au><au>Wu, Liyun</au><au>Chen, Yanhong</au><au>Ni, Hui</au><au>Xiao, Anfeng</au><au>Cai, Huinong</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of an extracellular biofunctional alginate lyase from marine Microbulbifer sp. ALW1 and antioxidant activity of enzymatic hydrolysates</atitle><jtitle>Microbiological research</jtitle><addtitle>Microbiol Res</addtitle><date>2016-01</date><risdate>2016</risdate><volume>182</volume><spage>49</spage><epage>58</epage><pages>49-58</pages><issn>0944-5013</issn><eissn>1618-0623</eissn><abstract>A novel alginate-degrading marine bacterium Microbulbifer sp. ALW1 was isolated from rotten brown alga. An extracellular alginate lyase was purified to electrophoretic homogeneity and had a molecular mass of about 26.0kDa determined by SDS-PAGE and size exclusion chromatography. This enzyme showed activities towards both polyguluronate and polymannuronate indicating its bifunctionality while with preference for the former substrate. Using sodium alginate as a substrate, strain ALW1 alginate lyase was optimally active at 45°C and pH 7.0. It was stable at 25°C, 30°C, 35°C and 40°C, but not stable at 50°C. This alginate lyase showed good stability over a broad pH range (5.0–9.0). The enzyme activity was increased to 5.1 times by adding NaCl to a final concentration of 0.5M. Strain ALW1 alginate lyase produced disaccharide (majority) and trisaccharide from alginate indicating that this enzyme could be a good tool for preparation of alginate oligosaccharides with low degree of polymerization (DP). The alginate oligosaccharides displayed the scavenging abilities towards radicals (DPPH, ABTS+ and hydroxyl) and the reducing power. Therefore, the hydrolysates exhibited the antioxidant activity and had potential as a natural antioxidant.</abstract><cop>Germany</cop><pub>Elsevier GmbH</pub><pmid>26686613</pmid><doi>10.1016/j.micres.2015.09.004</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0944-5013 |
| ispartof | Microbiological research, 2016-01, Vol.182, p.49-58 |
| issn | 0944-5013 1618-0623 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_1805510776 |
| source | MEDLINE; Elsevier ScienceDirect Journals; EZB-FREE-00999 freely available EZB journals |
| subjects | Alginate lyase Alginate oligosaccharides Alginates - metabolism Antioxidant activity Antioxidants - chemistry Antioxidants - metabolism Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Characterization Enzyme Stability Gammaproteobacteria - classification Gammaproteobacteria - enzymology Gammaproteobacteria - genetics Gammaproteobacteria - isolation & purification Glucuronic Acid - metabolism Hexuronic Acids - metabolism Hydrogen-Ion Concentration Microbulbifer sp Molecular Sequence Data Molecular Weight Phylogeny Polysaccharide-Lyases - chemistry Polysaccharide-Lyases - genetics Polysaccharide-Lyases - metabolism Seawater - microbiology Substrate Specificity Temperature |
| title | Characterization of an extracellular biofunctional alginate lyase from marine Microbulbifer sp. ALW1 and antioxidant activity of enzymatic hydrolysates |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-08T12%3A34%3A08IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Characterization%20of%20an%20extracellular%20biofunctional%20alginate%20lyase%20from%20marine%20Microbulbifer%20sp.%20ALW1%20and%20antioxidant%20activity%20of%20enzymatic%20hydrolysates&rft.jtitle=Microbiological%20research&rft.au=Zhu,%20Yanbing&rft.date=2016-01&rft.volume=182&rft.spage=49&rft.epage=58&rft.pages=49-58&rft.issn=0944-5013&rft.eissn=1618-0623&rft_id=info:doi/10.1016/j.micres.2015.09.004&rft_dat=%3Cproquest_cross%3E1751195503%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1751195503&rft_id=info:pmid/26686613&rft_els_id=S0944501315300082&rfr_iscdi=true |