Thermal characteristics and cadmium binding behavior of EC-ELP fusion polypeptides
•The cadmium binding affinity of EC-ELP fusion protein was examined by comparing the turbidity profiles to three other heavy metal ions.•The amount of Cd2+ adsorbed to the EC–ELP fusion proteins and the resulting Tt changes were explored according to the number of EC repeating units.•We observed whe...
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| Veröffentlicht in: | Enzyme and microbial technology 2020-10, Vol.140, p.109628-109628, Article 109628 |
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| creator | Choi, Heelak Han, Sung-Jin Won, Jong-In |
| description | •The cadmium binding affinity of EC-ELP fusion protein was examined by comparing the turbidity profiles to three other heavy metal ions.•The amount of Cd2+ adsorbed to the EC–ELP fusion proteins and the resulting Tt changes were explored according to the number of EC repeating units.•We observed whether our EC–ELP fusion proteins could be reused, after removing the adsorbed cadmium ions.
Elastin-like polypeptides (ELPs) are stimulus–responsive protein-based biopolymers that exhibit phase transition behavior. By joining them to synthetic phytochelatin (EC), EC–ELP fusion proteins with temperature sensitivity and metal-binding functionality were generated to remove heavy metal ions biologically. Three different EC domains (EC10, EC20, EC30) were incorporated into the ELP, and the EC–ELP fusion proteins were expressed in E. coli. Their thermal properties and metal binding abilities were then investigated according to the EC length. In addition, the feasibility of reusing EC–ELPs and the cadmium ion binding affinity of reused EC–ELPs were explored. |
| doi_str_mv | 10.1016/j.enzmictec.2020.109628 |
| format | Article |
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Elastin-like polypeptides (ELPs) are stimulus–responsive protein-based biopolymers that exhibit phase transition behavior. By joining them to synthetic phytochelatin (EC), EC–ELP fusion proteins with temperature sensitivity and metal-binding functionality were generated to remove heavy metal ions biologically. Three different EC domains (EC10, EC20, EC30) were incorporated into the ELP, and the EC–ELP fusion proteins were expressed in E. coli. Their thermal properties and metal binding abilities were then investigated according to the EC length. In addition, the feasibility of reusing EC–ELPs and the cadmium ion binding affinity of reused EC–ELPs were explored.</description><identifier>ISSN: 0141-0229</identifier><identifier>EISSN: 1879-0909</identifier><identifier>DOI: 10.1016/j.enzmictec.2020.109628</identifier><identifier>PMID: 32912688</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Cadmium - isolation & purification ; Cadmium - metabolism ; Cadmium adsorption ; Cloning, Molecular ; EC–ELP ; Elastin - chemistry ; Elastin - genetics ; Elastin - metabolism ; Elastin-like polypeptide (ELP) ; Escherichia coli - genetics ; Gene Expression ; Metals, Heavy - isolation & purification ; Metals, Heavy - metabolism ; Peptides - chemistry ; Peptides - genetics ; Peptides - metabolism ; Phase Transition ; Phytochelatins - chemistry ; Phytochelatins - genetics ; Phytochelatins - metabolism ; Recombinant Fusion Proteins - chemistry ; Recombinant Fusion Proteins - genetics ; Recombinant Fusion Proteins - metabolism ; Synthetic phytochelatin (EC) ; Temperature ; Water Pollutants, Chemical - isolation & purification ; Water Pollutants, Chemical - metabolism</subject><ispartof>Enzyme and microbial technology, 2020-10, Vol.140, p.109628-109628, Article 109628</ispartof><rights>2020 Elsevier Inc.</rights><rights>Copyright © 2020 Elsevier Inc. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c437t-ada15a7c9df86258829c7a935969fd7d2ae7b7415a334f30534517df5c28ba463</citedby><cites>FETCH-LOGICAL-c437t-ada15a7c9df86258829c7a935969fd7d2ae7b7415a334f30534517df5c28ba463</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0141022920301216$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/32912688$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Choi, Heelak</creatorcontrib><creatorcontrib>Han, Sung-Jin</creatorcontrib><creatorcontrib>Won, Jong-In</creatorcontrib><title>Thermal characteristics and cadmium binding behavior of EC-ELP fusion polypeptides</title><title>Enzyme and microbial technology</title><addtitle>Enzyme Microb Technol</addtitle><description>•The cadmium binding affinity of EC-ELP fusion protein was examined by comparing the turbidity profiles to three other heavy metal ions.•The amount of Cd2+ adsorbed to the EC–ELP fusion proteins and the resulting Tt changes were explored according to the number of EC repeating units.•We observed whether our EC–ELP fusion proteins could be reused, after removing the adsorbed cadmium ions.
Elastin-like polypeptides (ELPs) are stimulus–responsive protein-based biopolymers that exhibit phase transition behavior. By joining them to synthetic phytochelatin (EC), EC–ELP fusion proteins with temperature sensitivity and metal-binding functionality were generated to remove heavy metal ions biologically. Three different EC domains (EC10, EC20, EC30) were incorporated into the ELP, and the EC–ELP fusion proteins were expressed in E. coli. Their thermal properties and metal binding abilities were then investigated according to the EC length. In addition, the feasibility of reusing EC–ELPs and the cadmium ion binding affinity of reused EC–ELPs were explored.</description><subject>Cadmium - isolation & purification</subject><subject>Cadmium - metabolism</subject><subject>Cadmium adsorption</subject><subject>Cloning, Molecular</subject><subject>EC–ELP</subject><subject>Elastin - chemistry</subject><subject>Elastin - genetics</subject><subject>Elastin - metabolism</subject><subject>Elastin-like polypeptide (ELP)</subject><subject>Escherichia coli - genetics</subject><subject>Gene Expression</subject><subject>Metals, Heavy - isolation & purification</subject><subject>Metals, Heavy - metabolism</subject><subject>Peptides - chemistry</subject><subject>Peptides - genetics</subject><subject>Peptides - metabolism</subject><subject>Phase Transition</subject><subject>Phytochelatins - chemistry</subject><subject>Phytochelatins - genetics</subject><subject>Phytochelatins - metabolism</subject><subject>Recombinant Fusion Proteins - chemistry</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Synthetic phytochelatin (EC)</subject><subject>Temperature</subject><subject>Water Pollutants, Chemical - isolation & purification</subject><subject>Water Pollutants, Chemical - metabolism</subject><issn>0141-0229</issn><issn>1879-0909</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkF1LwzAUhoMobk7_gubSm84kTZvmcoz5AQNF5nVIk1OX0S-TVpi_3o7O3Xp14OU55-U8CN1RMqeEpg-7OdQ_lTMdmDkj7JDKlGVnaEozISMiiTxHU0I5jQhjcoKuQtgRMgScXKJJzCRlaZZN0ftmC77SJTZb7fVwz7vQOROwri022laur3DuauvqT5zDVn-7xuOmwKtltFq_4aIPrqlx25T7FtrOWQjX6KLQZYCb45yhj8fVZvkcrV-fXpaLdWR4LLpIW00TLYy0RZayJMuYNELLOJGpLKywTIPIBR-YOOZFTJKYJ1TYIjEsyzVP4xm6H--2vvnqIXSqcsFAWeoamj4oxjlNiZCCDqgYUeObEDwUqvWu0n6vKFEHoWqnTkLVQagahQ6bt8eSPq_Anvb-DA7AYgRgePXbgVfBOKgNWOfBdMo27t-SX7sliw4</recordid><startdate>202010</startdate><enddate>202010</enddate><creator>Choi, Heelak</creator><creator>Han, Sung-Jin</creator><creator>Won, Jong-In</creator><general>Elsevier Inc</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>7X8</scope></search><sort><creationdate>202010</creationdate><title>Thermal characteristics and cadmium binding behavior of EC-ELP fusion polypeptides</title><author>Choi, Heelak ; Han, Sung-Jin ; Won, Jong-In</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c437t-ada15a7c9df86258829c7a935969fd7d2ae7b7415a334f30534517df5c28ba463</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Cadmium - isolation & purification</topic><topic>Cadmium - metabolism</topic><topic>Cadmium adsorption</topic><topic>Cloning, Molecular</topic><topic>EC–ELP</topic><topic>Elastin - chemistry</topic><topic>Elastin - genetics</topic><topic>Elastin - metabolism</topic><topic>Elastin-like polypeptide (ELP)</topic><topic>Escherichia coli - genetics</topic><topic>Gene Expression</topic><topic>Metals, Heavy - isolation & purification</topic><topic>Metals, Heavy - metabolism</topic><topic>Peptides - chemistry</topic><topic>Peptides - genetics</topic><topic>Peptides - metabolism</topic><topic>Phase Transition</topic><topic>Phytochelatins - chemistry</topic><topic>Phytochelatins - genetics</topic><topic>Phytochelatins - metabolism</topic><topic>Recombinant Fusion Proteins - chemistry</topic><topic>Recombinant Fusion Proteins - genetics</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Synthetic phytochelatin (EC)</topic><topic>Temperature</topic><topic>Water Pollutants, Chemical - isolation & purification</topic><topic>Water Pollutants, Chemical - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Choi, Heelak</creatorcontrib><creatorcontrib>Han, Sung-Jin</creatorcontrib><creatorcontrib>Won, Jong-In</creatorcontrib><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><jtitle>Enzyme and microbial technology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Choi, Heelak</au><au>Han, Sung-Jin</au><au>Won, Jong-In</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Thermal characteristics and cadmium binding behavior of EC-ELP fusion polypeptides</atitle><jtitle>Enzyme and microbial technology</jtitle><addtitle>Enzyme Microb Technol</addtitle><date>2020-10</date><risdate>2020</risdate><volume>140</volume><spage>109628</spage><epage>109628</epage><pages>109628-109628</pages><artnum>109628</artnum><issn>0141-0229</issn><eissn>1879-0909</eissn><abstract>•The cadmium binding affinity of EC-ELP fusion protein was examined by comparing the turbidity profiles to three other heavy metal ions.•The amount of Cd2+ adsorbed to the EC–ELP fusion proteins and the resulting Tt changes were explored according to the number of EC repeating units.•We observed whether our EC–ELP fusion proteins could be reused, after removing the adsorbed cadmium ions.
Elastin-like polypeptides (ELPs) are stimulus–responsive protein-based biopolymers that exhibit phase transition behavior. By joining them to synthetic phytochelatin (EC), EC–ELP fusion proteins with temperature sensitivity and metal-binding functionality were generated to remove heavy metal ions biologically. Three different EC domains (EC10, EC20, EC30) were incorporated into the ELP, and the EC–ELP fusion proteins were expressed in E. coli. Their thermal properties and metal binding abilities were then investigated according to the EC length. In addition, the feasibility of reusing EC–ELPs and the cadmium ion binding affinity of reused EC–ELPs were explored.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>32912688</pmid><doi>10.1016/j.enzmictec.2020.109628</doi><tpages>1</tpages></addata></record> |
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| subjects | Cadmium - isolation & purification Cadmium - metabolism Cadmium adsorption Cloning, Molecular EC–ELP Elastin - chemistry Elastin - genetics Elastin - metabolism Elastin-like polypeptide (ELP) Escherichia coli - genetics Gene Expression Metals, Heavy - isolation & purification Metals, Heavy - metabolism Peptides - chemistry Peptides - genetics Peptides - metabolism Phase Transition Phytochelatins - chemistry Phytochelatins - genetics Phytochelatins - metabolism Recombinant Fusion Proteins - chemistry Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism Synthetic phytochelatin (EC) Temperature Water Pollutants, Chemical - isolation & purification Water Pollutants, Chemical - metabolism |
| title | Thermal characteristics and cadmium binding behavior of EC-ELP fusion polypeptides |
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