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Biochemical Characterization of a Novel Exo-Type PL7 Alginate Lyase VsAly7D from Marine Vibrio sp. QY108
Brown algae is a kind of renewable resource for biofuels production. As the major component of carbohydrate in the cell walls of brown algae, alginate can be degraded into unsaturated monosaccharide by exo-type alginate lyases, then converted into 4-deoxy-L- -5-hexoseulose uronate (DEH) by a non-enz...
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Published in: | International journal of molecular sciences 2021-08, Vol.22 (16), p.8402 |
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description | Brown algae is a kind of renewable resource for biofuels production. As the major component of carbohydrate in the cell walls of brown algae, alginate can be degraded into unsaturated monosaccharide by exo-type alginate lyases, then converted into 4-deoxy-L-
-5-hexoseulose uronate (DEH) by a non-enzyme reaction, which is an important raw material for the preparation of bioethanol. In our research, a novel exo-type alginate lyase, VsAly7D, belonging to the PL7 family was isolated from marine bacterium
sp. QY108 and recombinantly expressed in
. The purified VsAly7D demonstrated the highest activity at 35 °C, whereas it still maintained 46.5% and 83.1% of its initial activity at 20 °C and 30 °C, respectively. In addition, VsAly7D exhibited the maximum activity under alkaline conditions (pH 8.0), with the simultaneously remaining stability between pH 8.0 and 10.0. Compared with other reported exo-type enzymes, VsAly7D could efficiently degrade alginate, poly-β-D-mannuronate (polyM) and poly-α-L-guluronate (polyG) with highest specific activities (663.0 U/mg, 913.6 U/mg and 894.4 U/mg, respectively). These results showed that recombinant VsAly7D is a suitable tool enzyme for unsaturated alginate monosaccharide preparation and holds great promise for producing bioethanol from brown algae. |
doi_str_mv | 10.3390/ijms22168402 |
format | article |
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-5-hexoseulose uronate (DEH) by a non-enzyme reaction, which is an important raw material for the preparation of bioethanol. In our research, a novel exo-type alginate lyase, VsAly7D, belonging to the PL7 family was isolated from marine bacterium
sp. QY108 and recombinantly expressed in
. The purified VsAly7D demonstrated the highest activity at 35 °C, whereas it still maintained 46.5% and 83.1% of its initial activity at 20 °C and 30 °C, respectively. In addition, VsAly7D exhibited the maximum activity under alkaline conditions (pH 8.0), with the simultaneously remaining stability between pH 8.0 and 10.0. Compared with other reported exo-type enzymes, VsAly7D could efficiently degrade alginate, poly-β-D-mannuronate (polyM) and poly-α-L-guluronate (polyG) with highest specific activities (663.0 U/mg, 913.6 U/mg and 894.4 U/mg, respectively). These results showed that recombinant VsAly7D is a suitable tool enzyme for unsaturated alginate monosaccharide preparation and holds great promise for producing bioethanol from brown algae.</description><identifier>ISSN: 1422-0067</identifier><identifier>ISSN: 1661-6596</identifier><identifier>EISSN: 1422-0067</identifier><identifier>DOI: 10.3390/ijms22168402</identifier><identifier>PMID: 34445107</identifier><language>eng</language><publisher>Switzerland: MDPI AG</publisher><subject>Algae ; Alginate lyase ; Alginates ; Alginates - metabolism ; Alginic acid ; Amino Acid Sequence ; Amino acids ; Bacteria ; Bacterial Proteins - metabolism ; Biodiesel fuels ; Biofuels ; Carbohydrates ; Cell walls ; Cold ; E coli ; Enzymes ; Escherichia coli - metabolism ; Ethanol ; Glucuronic Acid - metabolism ; Hydrogen-Ion Concentration ; Industrial production ; Molecular weight ; Monosaccharides ; Monosaccharides - metabolism ; Phaeophyceae ; Phaeophyceae - microbiology ; Phylogenetics ; Polysaccharide-Lyases - metabolism ; Proteins ; Renewable resources ; Vibrio ; Vibrio - metabolism</subject><ispartof>International journal of molecular sciences, 2021-08, Vol.22 (16), p.8402</ispartof><rights>2021 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2021 by the authors. 2021</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c412t-856412e82ab2821e3decd5aa17888efcd55277657023ac40fe5727eb06fa2c73</citedby><cites>FETCH-LOGICAL-c412t-856412e82ab2821e3decd5aa17888efcd55277657023ac40fe5727eb06fa2c73</cites><orcidid>0000-0001-5706-7028</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.proquest.com/docview/2624241595/fulltextPDF?pq-origsite=primo$$EPDF$$P50$$Gproquest$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/2624241595?pq-origsite=primo$$EHTML$$P50$$Gproquest$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,25731,27901,27902,36989,36990,44566,53766,53768,74869</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/34445107$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zhang, Fengchao</creatorcontrib><creatorcontrib>Fu, Zheng</creatorcontrib><creatorcontrib>Tang, Luyao</creatorcontrib><creatorcontrib>Zhang, Zhelun</creatorcontrib><creatorcontrib>Han, Feng</creatorcontrib><creatorcontrib>Yu, Wengong</creatorcontrib><title>Biochemical Characterization of a Novel Exo-Type PL7 Alginate Lyase VsAly7D from Marine Vibrio sp. QY108</title><title>International journal of molecular sciences</title><addtitle>Int J Mol Sci</addtitle><description>Brown algae is a kind of renewable resource for biofuels production. As the major component of carbohydrate in the cell walls of brown algae, alginate can be degraded into unsaturated monosaccharide by exo-type alginate lyases, then converted into 4-deoxy-L-
-5-hexoseulose uronate (DEH) by a non-enzyme reaction, which is an important raw material for the preparation of bioethanol. In our research, a novel exo-type alginate lyase, VsAly7D, belonging to the PL7 family was isolated from marine bacterium
sp. QY108 and recombinantly expressed in
. The purified VsAly7D demonstrated the highest activity at 35 °C, whereas it still maintained 46.5% and 83.1% of its initial activity at 20 °C and 30 °C, respectively. In addition, VsAly7D exhibited the maximum activity under alkaline conditions (pH 8.0), with the simultaneously remaining stability between pH 8.0 and 10.0. Compared with other reported exo-type enzymes, VsAly7D could efficiently degrade alginate, poly-β-D-mannuronate (polyM) and poly-α-L-guluronate (polyG) with highest specific activities (663.0 U/mg, 913.6 U/mg and 894.4 U/mg, respectively). These results showed that recombinant VsAly7D is a suitable tool enzyme for unsaturated alginate monosaccharide preparation and holds great promise for producing bioethanol from brown algae.</description><subject>Algae</subject><subject>Alginate lyase</subject><subject>Alginates</subject><subject>Alginates - metabolism</subject><subject>Alginic acid</subject><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Bacteria</subject><subject>Bacterial Proteins - metabolism</subject><subject>Biodiesel fuels</subject><subject>Biofuels</subject><subject>Carbohydrates</subject><subject>Cell walls</subject><subject>Cold</subject><subject>E coli</subject><subject>Enzymes</subject><subject>Escherichia coli - metabolism</subject><subject>Ethanol</subject><subject>Glucuronic Acid - metabolism</subject><subject>Hydrogen-Ion Concentration</subject><subject>Industrial production</subject><subject>Molecular weight</subject><subject>Monosaccharides</subject><subject>Monosaccharides - metabolism</subject><subject>Phaeophyceae</subject><subject>Phaeophyceae - microbiology</subject><subject>Phylogenetics</subject><subject>Polysaccharide-Lyases - metabolism</subject><subject>Proteins</subject><subject>Renewable resources</subject><subject>Vibrio</subject><subject>Vibrio - metabolism</subject><issn>1422-0067</issn><issn>1661-6596</issn><issn>1422-0067</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>PIMPY</sourceid><recordid>eNpdkc1vEzEQxS0EoqVw44wsceHAtvasvXYuSCEUqBS-pAiJkzVxZhtHu-vU3lSkfz1GLVXKaUYzPz3Nm8fYSylO63oizsKmzwCysUrAI3YsFUAlRGMeH_RH7FnOGyGgBj15yo5qpZSWwhyz9fsQ_Zr64LHjszUm9COlcINjiAOPLUf-NV5Tx89_x2qx3xL_Pjd82l2GAUfi8z1m4j_ztNubD7xNsedfMIWhzMIyhcjz9pT_-CWFfc6etNhlenFXT9ji4_li9rmaf_t0MZvOK68kjJXVTalkAZdgQVK9Ir_SiNJYa6ktvQZjGm2KF_RKtKQNGFqKpkXwpj5h725lt7tlTytPw5iwc9sUekx7FzG4h5shrN1lvHa2nujyryLw5k4gxasd5dH1IXvqOhwo7rID3TRCgZSioK__Qzdxl4bizkEDCpTUE12ot7eUTzHnRO39MVK4vwm6wwQL_urQwD38L7L6D7xnlZU</recordid><startdate>20210805</startdate><enddate>20210805</enddate><creator>Zhang, Fengchao</creator><creator>Fu, Zheng</creator><creator>Tang, Luyao</creator><creator>Zhang, Zhelun</creator><creator>Han, Feng</creator><creator>Yu, Wengong</creator><general>MDPI AG</general><general>MDPI</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>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>K9.</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>MBDVC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0001-5706-7028</orcidid></search><sort><creationdate>20210805</creationdate><title>Biochemical Characterization of a Novel Exo-Type PL7 Alginate Lyase VsAly7D from Marine Vibrio sp. QY108</title><author>Zhang, Fengchao ; Fu, Zheng ; Tang, Luyao ; Zhang, Zhelun ; Han, Feng ; Yu, Wengong</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c412t-856412e82ab2821e3decd5aa17888efcd55277657023ac40fe5727eb06fa2c73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Algae</topic><topic>Alginate lyase</topic><topic>Alginates</topic><topic>Alginates - metabolism</topic><topic>Alginic acid</topic><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Bacteria</topic><topic>Bacterial Proteins - metabolism</topic><topic>Biodiesel fuels</topic><topic>Biofuels</topic><topic>Carbohydrates</topic><topic>Cell walls</topic><topic>Cold</topic><topic>E coli</topic><topic>Enzymes</topic><topic>Escherichia coli - metabolism</topic><topic>Ethanol</topic><topic>Glucuronic Acid - metabolism</topic><topic>Hydrogen-Ion Concentration</topic><topic>Industrial production</topic><topic>Molecular weight</topic><topic>Monosaccharides</topic><topic>Monosaccharides - metabolism</topic><topic>Phaeophyceae</topic><topic>Phaeophyceae - microbiology</topic><topic>Phylogenetics</topic><topic>Polysaccharide-Lyases - metabolism</topic><topic>Proteins</topic><topic>Renewable resources</topic><topic>Vibrio</topic><topic>Vibrio - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zhang, Fengchao</creatorcontrib><creatorcontrib>Fu, Zheng</creatorcontrib><creatorcontrib>Tang, Luyao</creatorcontrib><creatorcontrib>Zhang, Zhelun</creatorcontrib><creatorcontrib>Han, Feng</creatorcontrib><creatorcontrib>Yu, Wengong</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>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>PML(ProQuest Medical Library)</collection><collection>Research Library</collection><collection>Research Library (Corporate)</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>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>International journal of molecular sciences</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zhang, Fengchao</au><au>Fu, Zheng</au><au>Tang, Luyao</au><au>Zhang, Zhelun</au><au>Han, Feng</au><au>Yu, Wengong</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Biochemical Characterization of a Novel Exo-Type PL7 Alginate Lyase VsAly7D from Marine Vibrio sp. QY108</atitle><jtitle>International journal of molecular sciences</jtitle><addtitle>Int J Mol Sci</addtitle><date>2021-08-05</date><risdate>2021</risdate><volume>22</volume><issue>16</issue><spage>8402</spage><pages>8402-</pages><issn>1422-0067</issn><issn>1661-6596</issn><eissn>1422-0067</eissn><abstract>Brown algae is a kind of renewable resource for biofuels production. As the major component of carbohydrate in the cell walls of brown algae, alginate can be degraded into unsaturated monosaccharide by exo-type alginate lyases, then converted into 4-deoxy-L-
-5-hexoseulose uronate (DEH) by a non-enzyme reaction, which is an important raw material for the preparation of bioethanol. In our research, a novel exo-type alginate lyase, VsAly7D, belonging to the PL7 family was isolated from marine bacterium
sp. QY108 and recombinantly expressed in
. The purified VsAly7D demonstrated the highest activity at 35 °C, whereas it still maintained 46.5% and 83.1% of its initial activity at 20 °C and 30 °C, respectively. In addition, VsAly7D exhibited the maximum activity under alkaline conditions (pH 8.0), with the simultaneously remaining stability between pH 8.0 and 10.0. Compared with other reported exo-type enzymes, VsAly7D could efficiently degrade alginate, poly-β-D-mannuronate (polyM) and poly-α-L-guluronate (polyG) with highest specific activities (663.0 U/mg, 913.6 U/mg and 894.4 U/mg, respectively). These results showed that recombinant VsAly7D is a suitable tool enzyme for unsaturated alginate monosaccharide preparation and holds great promise for producing bioethanol from brown algae.</abstract><cop>Switzerland</cop><pub>MDPI AG</pub><pmid>34445107</pmid><doi>10.3390/ijms22168402</doi><orcidid>https://orcid.org/0000-0001-5706-7028</orcidid><oa>free_for_read</oa></addata></record> |
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subjects | Algae Alginate lyase Alginates Alginates - metabolism Alginic acid Amino Acid Sequence Amino acids Bacteria Bacterial Proteins - metabolism Biodiesel fuels Biofuels Carbohydrates Cell walls Cold E coli Enzymes Escherichia coli - metabolism Ethanol Glucuronic Acid - metabolism Hydrogen-Ion Concentration Industrial production Molecular weight Monosaccharides Monosaccharides - metabolism Phaeophyceae Phaeophyceae - microbiology Phylogenetics Polysaccharide-Lyases - metabolism Proteins Renewable resources Vibrio Vibrio - metabolism |
title | Biochemical Characterization of a Novel Exo-Type PL7 Alginate Lyase VsAly7D from Marine Vibrio sp. QY108 |
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