Optimization of cold-adapted alpha-galactosidase expression in Escherichia coli
α-Galactosidase (α-PsGal) of the cold-adapted marine bacterium Pseudoalteromonas sp. KMM 701 was cloned into the pET-40b(+) vector to study its properties and to develop an effective method for modifying human B-erythrocytes into O-blood group. The use of heat-shock as a pre-induction treatment, IPT...
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| Veröffentlicht in: | Protein expression and purification 2016-07, Vol.123, p.14-18 |
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| container_title | Protein expression and purification |
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| creator | Golotin, V.A. Balabanova, L.A. Noskova, Yu. A. Slepchenko, L.V. Bakunina, I. Yu Vorobieva, N.S. Terenteva, N.A. Rasskazov, V.A. |
| description | α-Galactosidase (α-PsGal) of the cold-adapted marine bacterium Pseudoalteromonas sp. KMM 701 was cloned into the pET-40b(+) vector to study its properties and to develop an effective method for modifying human B-erythrocytes into O-blood group. The use of heat-shock as a pre-induction treatment, IPTG concentration of 0.2 mM and post-induction cultivation at 18 °C for 20 h in the developed MX-medium allowed increasing the recombinant Escherichia coli Rosetta (DE3)/40Gal strain productivity up to 30 times and the total soluble α-PsGal yield up to 40 times.
•The expression of recombinant alpha-galactosidase α-PsGal from marine bacterium Pseudoalteromonas sp. was optimized.•The parameters for the maximal α-PsGal yield in soluble form in E. coli were selected.•A novel medium MX for the expression in E.coli was suggested for enhancing recombinant soluble protein production. |
| doi_str_mv | 10.1016/j.pep.2016.03.006 |
| format | Article |
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•The expression of recombinant alpha-galactosidase α-PsGal from marine bacterium Pseudoalteromonas sp. was optimized.•The parameters for the maximal α-PsGal yield in soluble form in E. coli were selected.•A novel medium MX for the expression in E.coli was suggested for enhancing recombinant soluble protein production.</description><identifier>ISSN: 1046-5928</identifier><identifier>EISSN: 1096-0279</identifier><identifier>DOI: 10.1016/j.pep.2016.03.006</identifier><identifier>PMID: 27033343</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Acclimatization ; Alpha-galactosidase ; alpha-Galactosidase - genetics ; alpha-Galactosidase - metabolism ; Cell Culture Techniques - methods ; Cloning, Molecular - methods ; Cold Temperature ; Erythrocytes - metabolism ; Escherichia coli ; Escherichia coli - genetics ; Escherichia coli - growth & development ; Escherichia coli - metabolism ; Heat-Shock Response ; Humans ; Prokaryotic gene expression ; Pseudoalteromonas ; Pseudoalteromonas - enzymology ; Pseudoalteromonas - genetics ; Pseudoalteromonas sp ; Psychrophilic enzyme ; Recombinant Proteins - genetics ; Recombinant Proteins - metabolism</subject><ispartof>Protein expression and purification, 2016-07, Vol.123, p.14-18</ispartof><rights>2016 Elsevier Inc.</rights><rights>Copyright © 2016 Elsevier Inc. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c386t-a549209bc65d7582975cd867843a174d8c4c497001f311d839a54ace89322fd83</citedby><cites>FETCH-LOGICAL-c386t-a549209bc65d7582975cd867843a174d8c4c497001f311d839a54ace89322fd83</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S1046592816300419$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65534</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27033343$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Golotin, V.A.</creatorcontrib><creatorcontrib>Balabanova, L.A.</creatorcontrib><creatorcontrib>Noskova, Yu. A.</creatorcontrib><creatorcontrib>Slepchenko, L.V.</creatorcontrib><creatorcontrib>Bakunina, I. Yu</creatorcontrib><creatorcontrib>Vorobieva, N.S.</creatorcontrib><creatorcontrib>Terenteva, N.A.</creatorcontrib><creatorcontrib>Rasskazov, V.A.</creatorcontrib><title>Optimization of cold-adapted alpha-galactosidase expression in Escherichia coli</title><title>Protein expression and purification</title><addtitle>Protein Expr Purif</addtitle><description>α-Galactosidase (α-PsGal) of the cold-adapted marine bacterium Pseudoalteromonas sp. KMM 701 was cloned into the pET-40b(+) vector to study its properties and to develop an effective method for modifying human B-erythrocytes into O-blood group. The use of heat-shock as a pre-induction treatment, IPTG concentration of 0.2 mM and post-induction cultivation at 18 °C for 20 h in the developed MX-medium allowed increasing the recombinant Escherichia coli Rosetta (DE3)/40Gal strain productivity up to 30 times and the total soluble α-PsGal yield up to 40 times.
•The expression of recombinant alpha-galactosidase α-PsGal from marine bacterium Pseudoalteromonas sp. was optimized.•The parameters for the maximal α-PsGal yield in soluble form in E. coli were selected.•A novel medium MX for the expression in E.coli was suggested for enhancing recombinant soluble protein production.</description><subject>Acclimatization</subject><subject>Alpha-galactosidase</subject><subject>alpha-Galactosidase - genetics</subject><subject>alpha-Galactosidase - metabolism</subject><subject>Cell Culture Techniques - methods</subject><subject>Cloning, Molecular - methods</subject><subject>Cold Temperature</subject><subject>Erythrocytes - metabolism</subject><subject>Escherichia coli</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli - growth & development</subject><subject>Escherichia coli - metabolism</subject><subject>Heat-Shock Response</subject><subject>Humans</subject><subject>Prokaryotic gene expression</subject><subject>Pseudoalteromonas</subject><subject>Pseudoalteromonas - enzymology</subject><subject>Pseudoalteromonas - genetics</subject><subject>Pseudoalteromonas sp</subject><subject>Psychrophilic enzyme</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - metabolism</subject><issn>1046-5928</issn><issn>1096-0279</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkMtOwzAQRS0EoqXwAWxQlmwS_Ej8ECtUlYdUqRtYW649oa7SJtgpAr4eRy0sYTUz0rlXo4PQJcEFwYTfrIsOuoKmtcCswJgfoTHBiueYCnU87CXPK0XlCJ3FuMaYEI6rUzSiAjPGSjZGi0XX-43_Mr1vt1lbZ7ZtXG6c6XpwmWm6lclfTWNs30bvTIQMProAMQ6432azaFcQvF15M0T9OTqpTRPh4jAn6OV-9jx9zOeLh6fp3Ty3TPI-N1WpKFZLyysnKkmVqKyTXMiSGSJKJ21pSyXSxzUjxEmmUsJYkIpRWqd7gq73vV1o33YQe73x0ULTmC20u6iJxKlOCU7_R4WUlHJORELJHrWhjTFArbvgNyZ8aoL1oFyvdVKuB-UaM52Up8zVoX633ID7Tfw4TsDtHoDk491D0NF62FpwPoDttWv9H_XfIDiQQw</recordid><startdate>201607</startdate><enddate>201607</enddate><creator>Golotin, V.A.</creator><creator>Balabanova, L.A.</creator><creator>Noskova, Yu. A.</creator><creator>Slepchenko, L.V.</creator><creator>Bakunina, I. Yu</creator><creator>Vorobieva, N.S.</creator><creator>Terenteva, N.A.</creator><creator>Rasskazov, V.A.</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><scope>7QL</scope><scope>C1K</scope></search><sort><creationdate>201607</creationdate><title>Optimization of cold-adapted alpha-galactosidase expression in Escherichia coli</title><author>Golotin, V.A. ; Balabanova, L.A. ; Noskova, Yu. A. ; Slepchenko, L.V. ; Bakunina, I. Yu ; Vorobieva, N.S. ; Terenteva, N.A. ; Rasskazov, V.A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c386t-a549209bc65d7582975cd867843a174d8c4c497001f311d839a54ace89322fd83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Acclimatization</topic><topic>Alpha-galactosidase</topic><topic>alpha-Galactosidase - genetics</topic><topic>alpha-Galactosidase - metabolism</topic><topic>Cell Culture Techniques - methods</topic><topic>Cloning, Molecular - methods</topic><topic>Cold Temperature</topic><topic>Erythrocytes - metabolism</topic><topic>Escherichia coli</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli - growth & development</topic><topic>Escherichia coli - metabolism</topic><topic>Heat-Shock Response</topic><topic>Humans</topic><topic>Prokaryotic gene expression</topic><topic>Pseudoalteromonas</topic><topic>Pseudoalteromonas - enzymology</topic><topic>Pseudoalteromonas - genetics</topic><topic>Pseudoalteromonas sp</topic><topic>Psychrophilic enzyme</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Golotin, V.A.</creatorcontrib><creatorcontrib>Balabanova, L.A.</creatorcontrib><creatorcontrib>Noskova, Yu. A.</creatorcontrib><creatorcontrib>Slepchenko, L.V.</creatorcontrib><creatorcontrib>Bakunina, I. Yu</creatorcontrib><creatorcontrib>Vorobieva, N.S.</creatorcontrib><creatorcontrib>Terenteva, N.A.</creatorcontrib><creatorcontrib>Rasskazov, V.A.</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><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><jtitle>Protein expression and purification</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Golotin, V.A.</au><au>Balabanova, L.A.</au><au>Noskova, Yu. A.</au><au>Slepchenko, L.V.</au><au>Bakunina, I. Yu</au><au>Vorobieva, N.S.</au><au>Terenteva, N.A.</au><au>Rasskazov, V.A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Optimization of cold-adapted alpha-galactosidase expression in Escherichia coli</atitle><jtitle>Protein expression and purification</jtitle><addtitle>Protein Expr Purif</addtitle><date>2016-07</date><risdate>2016</risdate><volume>123</volume><spage>14</spage><epage>18</epage><pages>14-18</pages><issn>1046-5928</issn><eissn>1096-0279</eissn><abstract>α-Galactosidase (α-PsGal) of the cold-adapted marine bacterium Pseudoalteromonas sp. KMM 701 was cloned into the pET-40b(+) vector to study its properties and to develop an effective method for modifying human B-erythrocytes into O-blood group. The use of heat-shock as a pre-induction treatment, IPTG concentration of 0.2 mM and post-induction cultivation at 18 °C for 20 h in the developed MX-medium allowed increasing the recombinant Escherichia coli Rosetta (DE3)/40Gal strain productivity up to 30 times and the total soluble α-PsGal yield up to 40 times.
•The expression of recombinant alpha-galactosidase α-PsGal from marine bacterium Pseudoalteromonas sp. was optimized.•The parameters for the maximal α-PsGal yield in soluble form in E. coli were selected.•A novel medium MX for the expression in E.coli was suggested for enhancing recombinant soluble protein production.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>27033343</pmid><doi>10.1016/j.pep.2016.03.006</doi><tpages>5</tpages></addata></record> |
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| subjects | Acclimatization Alpha-galactosidase alpha-Galactosidase - genetics alpha-Galactosidase - metabolism Cell Culture Techniques - methods Cloning, Molecular - methods Cold Temperature Erythrocytes - metabolism Escherichia coli Escherichia coli - genetics Escherichia coli - growth & development Escherichia coli - metabolism Heat-Shock Response Humans Prokaryotic gene expression Pseudoalteromonas Pseudoalteromonas - enzymology Pseudoalteromonas - genetics Pseudoalteromonas sp Psychrophilic enzyme Recombinant Proteins - genetics Recombinant Proteins - metabolism |
| title | Optimization of cold-adapted alpha-galactosidase expression in Escherichia coli |
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