Characterization of a recombinant endo-type alginate lyase (Alg7D) from Saccharophagus degradans
A gene, alg7D, from Saccharophagus degradans, coding for a putative alginate lyase belonging to the family of polysaccharide lyase-7, was overexpressed in Escherichia coli. The properties of the recombinant Alg7D were characterized. The enzyme endolytically depolymerized alginate by β-elimination in...
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| Veröffentlicht in: | Biotechnology letters 2012-06, Vol.34 (6), p.1087-1092 |
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| container_title | Biotechnology letters |
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| creator | Kim, Hee Taek Ko, Hyeok-Jin Kim, Nahyun Kim, Duwoon Lee, Dongho Choi, In-Geol Woo, Hee Chul Kim, Myoung Dong Kim, Kyoung Heon |
| description | A gene, alg7D, from Saccharophagus degradans, coding for a putative alginate lyase belonging to the family of polysaccharide lyase-7, was overexpressed in Escherichia coli. The properties of the recombinant Alg7D were characterized. The enzyme endolytically depolymerized alginate by β-elimination into oligo-alginates with degrees of polymerization of 2–5. Its activity was maximal at 50°C and pH 7 and was slightly increased in the presence of Na+. The K M , V max , k cat , and k cat /K M values were: 3 mg ml−1, 6.2 U mg−1, 1.9 × 10−2 s−1, and 6.3 × 10−3 mg−1 ml s−1, respectively. |
| doi_str_mv | 10.1007/s10529-012-0876-9 |
| format | Article |
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The properties of the recombinant Alg7D were characterized. The enzyme endolytically depolymerized alginate by β-elimination into oligo-alginates with degrees of polymerization of 2–5. Its activity was maximal at 50°C and pH 7 and was slightly increased in the presence of Na+. The K M , V max , k cat , and k cat /K M values were: 3 mg ml−1, 6.2 U mg−1, 1.9 × 10−2 s−1, and 6.3 × 10−3 mg−1 ml s−1, respectively.</description><identifier>ISSN: 0141-5492</identifier><identifier>EISSN: 1573-6776</identifier><identifier>DOI: 10.1007/s10529-012-0876-9</identifier><identifier>PMID: 22391735</identifier><identifier>CODEN: BILED3</identifier><language>eng</language><publisher>Dordrecht: Springer-Verlag</publisher><subject>Alginates ; Alginates - metabolism ; Alteromonadaceae - enzymology ; Alteromonadaceae - genetics ; Applied Microbiology ; Bacteria ; Biochemistry ; Biological and medical sciences ; Biomedical and Life Sciences ; Biotechnology ; Degradation ; E coli ; Enzyme Stability ; Enzymes ; Escherichia coli ; Escherichia coli - genetics ; Fundamental and applied biological sciences. Psychology ; Gene Expression ; gene overexpression ; Genes ; Glucuronic Acid - metabolism ; Hexuronic Acids - metabolism ; Hydrogen-Ion Concentration ; Kinetics ; Life Sciences ; Magnesium ; Microbiology ; Oligosaccharides - metabolism ; Original Research Paper ; polymerization ; Polysaccharide-Lyases - chemistry ; Polysaccharide-Lyases - genetics ; Polysaccharide-Lyases - metabolism ; Recombinant ; Recombinant Proteins - chemistry ; Recombinant Proteins - genetics ; Recombinant Proteins - metabolism ; Temperature</subject><ispartof>Biotechnology letters, 2012-06, Vol.34 (6), p.1087-1092</ispartof><rights>Springer Science+Business Media B.V. 2012</rights><rights>2015 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c582t-421110e454e5ac297bb5c594b91ddababda5c93a11c5c8bdb1403fa83bcbdac93</citedby><cites>FETCH-LOGICAL-c582t-421110e454e5ac297bb5c594b91ddababda5c93a11c5c8bdb1403fa83bcbdac93</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s10529-012-0876-9$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s10529-012-0876-9$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=25850536$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22391735$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kim, Hee Taek</creatorcontrib><creatorcontrib>Ko, Hyeok-Jin</creatorcontrib><creatorcontrib>Kim, Nahyun</creatorcontrib><creatorcontrib>Kim, Duwoon</creatorcontrib><creatorcontrib>Lee, Dongho</creatorcontrib><creatorcontrib>Choi, In-Geol</creatorcontrib><creatorcontrib>Woo, Hee Chul</creatorcontrib><creatorcontrib>Kim, Myoung Dong</creatorcontrib><creatorcontrib>Kim, Kyoung Heon</creatorcontrib><title>Characterization of a recombinant endo-type alginate lyase (Alg7D) from Saccharophagus degradans</title><title>Biotechnology letters</title><addtitle>Biotechnol Lett</addtitle><addtitle>Biotechnol Lett</addtitle><description>A gene, alg7D, from Saccharophagus degradans, coding for a putative alginate lyase belonging to the family of polysaccharide lyase-7, was overexpressed in Escherichia coli. The properties of the recombinant Alg7D were characterized. The enzyme endolytically depolymerized alginate by β-elimination into oligo-alginates with degrees of polymerization of 2–5. Its activity was maximal at 50°C and pH 7 and was slightly increased in the presence of Na+. The K M , V max , k cat , and k cat /K M values were: 3 mg ml−1, 6.2 U mg−1, 1.9 × 10−2 s−1, and 6.3 × 10−3 mg−1 ml s−1, respectively.</description><subject>Alginates</subject><subject>Alginates - metabolism</subject><subject>Alteromonadaceae - enzymology</subject><subject>Alteromonadaceae - genetics</subject><subject>Applied Microbiology</subject><subject>Bacteria</subject><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Biomedical and Life Sciences</subject><subject>Biotechnology</subject><subject>Degradation</subject><subject>E coli</subject><subject>Enzyme Stability</subject><subject>Enzymes</subject><subject>Escherichia coli</subject><subject>Escherichia coli - genetics</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Expression</subject><subject>gene overexpression</subject><subject>Genes</subject><subject>Glucuronic Acid - metabolism</subject><subject>Hexuronic Acids - metabolism</subject><subject>Hydrogen-Ion Concentration</subject><subject>Kinetics</subject><subject>Life Sciences</subject><subject>Magnesium</subject><subject>Microbiology</subject><subject>Oligosaccharides - metabolism</subject><subject>Original Research Paper</subject><subject>polymerization</subject><subject>Polysaccharide-Lyases - chemistry</subject><subject>Polysaccharide-Lyases - genetics</subject><subject>Polysaccharide-Lyases - metabolism</subject><subject>Recombinant</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - metabolism</subject><subject>Temperature</subject><issn>0141-5492</issn><issn>1573-6776</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNqNkktv1TAQhS0EoreFH8AGLCGksgh4_IjjZXUpD6kSi9J1GDtOmio3vtjJ4vLrcZTLQ0g8VpZ8vjkzozOEPAH2ChjTrxMwxU3BgBes0mVh7pENKC2KUuvyPtkwkFAoafgJOU3pjjFmNNMPyQnnwoAWakM-b28xopt87L_i1IeRhpYijd6Fne1HHCfqxyYU02HvKQ5d_po8HQ6YPD2_GDr95iVtY9jRa3QuW4X9LXZzoo3vIjY4pkfkQYtD8o-P7xm5eXv5afu-uPr47sP24qpwquJTITkAMC-V9AodN9pa5ZSR1kDToEXboHJGIIBTrrKNBclEi5WwLktZOSPnq-8-hi-zT1O965Pzw4CjD3OqoaxUBVKX-t8oA20qBcz8D8q4KMGIjD7_Db0LcxzzzgslpBSmLDMFK-ViSCn6tt7HfofxkKF6CbVeQ61zqPUSar0M8fToPNudb35UfE8xAy-OACaHQxtxdH36yalKMSWW5nzlUpbGzsdfR_xz92drUYuhxi5m45trnk8rn5MsGdd_JbjWlRbfAI2ayo8</recordid><startdate>20120601</startdate><enddate>20120601</enddate><creator>Kim, Hee Taek</creator><creator>Ko, Hyeok-Jin</creator><creator>Kim, Nahyun</creator><creator>Kim, Duwoon</creator><creator>Lee, Dongho</creator><creator>Choi, In-Geol</creator><creator>Woo, Hee Chul</creator><creator>Kim, Myoung Dong</creator><creator>Kim, Kyoung Heon</creator><general>Springer-Verlag</general><general>Springer Netherlands</general><general>Springer</general><general>Springer Nature B.V</general><scope>FBQ</scope><scope>IQODW</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>3V.</scope><scope>7QL</scope><scope>7QR</scope><scope>7T7</scope><scope>7TB</scope><scope>7U5</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</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>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>L6V</scope><scope>L7M</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PTHSS</scope><scope>Q9U</scope><scope>7X8</scope><scope>7QO</scope><scope>RC3</scope></search><sort><creationdate>20120601</creationdate><title>Characterization of a recombinant endo-type alginate lyase (Alg7D) from Saccharophagus degradans</title><author>Kim, Hee Taek ; Ko, Hyeok-Jin ; Kim, Nahyun ; Kim, Duwoon ; Lee, Dongho ; Choi, In-Geol ; Woo, Hee Chul ; Kim, Myoung Dong ; Kim, Kyoung Heon</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c582t-421110e454e5ac297bb5c594b91ddababda5c93a11c5c8bdb1403fa83bcbdac93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Alginates</topic><topic>Alginates - metabolism</topic><topic>Alteromonadaceae - enzymology</topic><topic>Alteromonadaceae - genetics</topic><topic>Applied Microbiology</topic><topic>Bacteria</topic><topic>Biochemistry</topic><topic>Biological and medical sciences</topic><topic>Biomedical and Life Sciences</topic><topic>Biotechnology</topic><topic>Degradation</topic><topic>E coli</topic><topic>Enzyme Stability</topic><topic>Enzymes</topic><topic>Escherichia coli</topic><topic>Escherichia coli - genetics</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Expression</topic><topic>gene overexpression</topic><topic>Genes</topic><topic>Glucuronic Acid - metabolism</topic><topic>Hexuronic Acids - metabolism</topic><topic>Hydrogen-Ion Concentration</topic><topic>Kinetics</topic><topic>Life Sciences</topic><topic>Magnesium</topic><topic>Microbiology</topic><topic>Oligosaccharides - metabolism</topic><topic>Original Research Paper</topic><topic>polymerization</topic><topic>Polysaccharide-Lyases - chemistry</topic><topic>Polysaccharide-Lyases - genetics</topic><topic>Polysaccharide-Lyases - metabolism</topic><topic>Recombinant</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - metabolism</topic><topic>Temperature</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kim, Hee Taek</creatorcontrib><creatorcontrib>Ko, Hyeok-Jin</creatorcontrib><creatorcontrib>Kim, Nahyun</creatorcontrib><creatorcontrib>Kim, Duwoon</creatorcontrib><creatorcontrib>Lee, Dongho</creatorcontrib><creatorcontrib>Choi, In-Geol</creatorcontrib><creatorcontrib>Woo, Hee Chul</creatorcontrib><creatorcontrib>Kim, Myoung Dong</creatorcontrib><creatorcontrib>Kim, Kyoung Heon</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><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>Bacteriology Abstracts (Microbiology B)</collection><collection>Chemoreception Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Mechanical & Transportation Engineering Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</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>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 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>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Engineering Collection</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Engineering Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Engineering Collection</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>Biotechnology Research Abstracts</collection><collection>Genetics Abstracts</collection><jtitle>Biotechnology letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kim, Hee Taek</au><au>Ko, Hyeok-Jin</au><au>Kim, Nahyun</au><au>Kim, Duwoon</au><au>Lee, Dongho</au><au>Choi, In-Geol</au><au>Woo, Hee Chul</au><au>Kim, Myoung Dong</au><au>Kim, Kyoung Heon</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of a recombinant endo-type alginate lyase (Alg7D) from Saccharophagus degradans</atitle><jtitle>Biotechnology letters</jtitle><stitle>Biotechnol Lett</stitle><addtitle>Biotechnol Lett</addtitle><date>2012-06-01</date><risdate>2012</risdate><volume>34</volume><issue>6</issue><spage>1087</spage><epage>1092</epage><pages>1087-1092</pages><issn>0141-5492</issn><eissn>1573-6776</eissn><coden>BILED3</coden><abstract>A gene, alg7D, from Saccharophagus degradans, coding for a putative alginate lyase belonging to the family of polysaccharide lyase-7, was overexpressed in Escherichia coli. The properties of the recombinant Alg7D were characterized. The enzyme endolytically depolymerized alginate by β-elimination into oligo-alginates with degrees of polymerization of 2–5. Its activity was maximal at 50°C and pH 7 and was slightly increased in the presence of Na+. The K M , V max , k cat , and k cat /K M values were: 3 mg ml−1, 6.2 U mg−1, 1.9 × 10−2 s−1, and 6.3 × 10−3 mg−1 ml s−1, respectively.</abstract><cop>Dordrecht</cop><pub>Springer-Verlag</pub><pmid>22391735</pmid><doi>10.1007/s10529-012-0876-9</doi><tpages>6</tpages></addata></record> |
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| subjects | Alginates Alginates - metabolism Alteromonadaceae - enzymology Alteromonadaceae - genetics Applied Microbiology Bacteria Biochemistry Biological and medical sciences Biomedical and Life Sciences Biotechnology Degradation E coli Enzyme Stability Enzymes Escherichia coli Escherichia coli - genetics Fundamental and applied biological sciences. Psychology Gene Expression gene overexpression Genes Glucuronic Acid - metabolism Hexuronic Acids - metabolism Hydrogen-Ion Concentration Kinetics Life Sciences Magnesium Microbiology Oligosaccharides - metabolism Original Research Paper polymerization Polysaccharide-Lyases - chemistry Polysaccharide-Lyases - genetics Polysaccharide-Lyases - metabolism Recombinant Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism Temperature |
| title | Characterization of a recombinant endo-type alginate lyase (Alg7D) from Saccharophagus degradans |
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