Cloning and expression of a gene with phospholipase B activity from Pseudomonas fluorescens in Escherichia coli
► This is the first report on the cloning of a plb gene from the genus Pseudomonas. ► Pf-PLB from P. fluorescens BIT-18 is a member of a new phospholipase B family. ► The overproduction of Pf-PLB is of interest for the applications in many industries. A gene from Pseudomonasfluorescens BIT-18 encodi...
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| Veröffentlicht in: | Bioresource technology 2012-01, Vol.104, p.518-522 |
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| creator | Jiang, Fangyan Huang, Shen Imadad, Kaleem Li, Chun |
| description | ► This is the first report on the cloning of a plb gene from the genus Pseudomonas. ► Pf-PLB from P. fluorescens BIT-18 is a member of a new phospholipase B family. ► The overproduction of Pf-PLB is of interest for the applications in many industries.
A gene from Pseudomonasfluorescens BIT-18 encoding a protein with phospholipase B activity (Pf-PLB) was cloned in E. coli BL21 (DE3). The open reading frame consists of 1272bp and potentially encodes a protein of 423 amino acid residues with a calculated molecular mass of 45.8kDa. The nucleotide sequence of Pf-PLB is 45%, 42%, 41%, 40%, 33%, and 31% identical to that of Bifidobacteriumanimals, Mycobacteriumparascrofulaceum, Acidobacteriumcapsulatum, Lactobacillusjohnsonii, Moraxellabovis, and Moraxellacatarrhalis, respectively. The His-tagged protein was purified by affinity chromatography and the eluted protein hydrolyzed both the 1- and 2-ester bond of phosphatidylcholine. The recombinant Pf-PLB had optimal activity at pH 6.0 and 30°C, and it showed 20.1% higher efficiency in the conversion rate of the phosphorus content than the wild-type. |
| doi_str_mv | 10.1016/j.biortech.2011.09.112 |
| format | Article |
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A gene from Pseudomonasfluorescens BIT-18 encoding a protein with phospholipase B activity (Pf-PLB) was cloned in E. coli BL21 (DE3). The open reading frame consists of 1272bp and potentially encodes a protein of 423 amino acid residues with a calculated molecular mass of 45.8kDa. The nucleotide sequence of Pf-PLB is 45%, 42%, 41%, 40%, 33%, and 31% identical to that of Bifidobacteriumanimals, Mycobacteriumparascrofulaceum, Acidobacteriumcapsulatum, Lactobacillusjohnsonii, Moraxellabovis, and Moraxellacatarrhalis, respectively. The His-tagged protein was purified by affinity chromatography and the eluted protein hydrolyzed both the 1- and 2-ester bond of phosphatidylcholine. The recombinant Pf-PLB had optimal activity at pH 6.0 and 30°C, and it showed 20.1% higher efficiency in the conversion rate of the phosphorus content than the wild-type.</description><identifier>ISSN: 0960-8524</identifier><identifier>EISSN: 1873-2976</identifier><identifier>DOI: 10.1016/j.biortech.2011.09.112</identifier><identifier>PMID: 22078969</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Cloning, Molecular - methods ; Enzyme Activation ; Enzyme Stability ; Escherichia coli ; Escherichia coli - enzymology ; Escherichia coli - metabolism ; Escherichiacoli ; Expression ; Gene cloning ; Gene Expression Regulation, Bacterial - physiology ; Lysophospholipase - chemistry ; Lysophospholipase - genetics ; Lysophospholipase - metabolism ; Phospholipase B ; Pseudomonas fluorescens ; Pseudomonas fluorescens - enzymology ; Pseudomonas fluorescens - metabolism ; Pseudomonasfluorescens ; Recombinant Proteins - metabolism ; Substrate Specificity</subject><ispartof>Bioresource technology, 2012-01, Vol.104, p.518-522</ispartof><rights>2011 Elsevier Ltd</rights><rights>Copyright © 2011 Elsevier Ltd. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c399t-159b10ef55b2e0d8aa00c44656852c49ef291328c843ed16092798c6a51e90763</citedby><cites>FETCH-LOGICAL-c399t-159b10ef55b2e0d8aa00c44656852c49ef291328c843ed16092798c6a51e90763</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.biortech.2011.09.112$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,778,782,3539,27907,27908,45978</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22078969$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Jiang, Fangyan</creatorcontrib><creatorcontrib>Huang, Shen</creatorcontrib><creatorcontrib>Imadad, Kaleem</creatorcontrib><creatorcontrib>Li, Chun</creatorcontrib><title>Cloning and expression of a gene with phospholipase B activity from Pseudomonas fluorescens in Escherichia coli</title><title>Bioresource technology</title><addtitle>Bioresour Technol</addtitle><description>► This is the first report on the cloning of a plb gene from the genus Pseudomonas. ► Pf-PLB from P. fluorescens BIT-18 is a member of a new phospholipase B family. ► The overproduction of Pf-PLB is of interest for the applications in many industries.
A gene from Pseudomonasfluorescens BIT-18 encoding a protein with phospholipase B activity (Pf-PLB) was cloned in E. coli BL21 (DE3). The open reading frame consists of 1272bp and potentially encodes a protein of 423 amino acid residues with a calculated molecular mass of 45.8kDa. The nucleotide sequence of Pf-PLB is 45%, 42%, 41%, 40%, 33%, and 31% identical to that of Bifidobacteriumanimals, Mycobacteriumparascrofulaceum, Acidobacteriumcapsulatum, Lactobacillusjohnsonii, Moraxellabovis, and Moraxellacatarrhalis, respectively. The His-tagged protein was purified by affinity chromatography and the eluted protein hydrolyzed both the 1- and 2-ester bond of phosphatidylcholine. The recombinant Pf-PLB had optimal activity at pH 6.0 and 30°C, and it showed 20.1% higher efficiency in the conversion rate of the phosphorus content than the wild-type.</description><subject>Cloning, Molecular - methods</subject><subject>Enzyme Activation</subject><subject>Enzyme Stability</subject><subject>Escherichia coli</subject><subject>Escherichia coli - enzymology</subject><subject>Escherichia coli - metabolism</subject><subject>Escherichiacoli</subject><subject>Expression</subject><subject>Gene cloning</subject><subject>Gene Expression Regulation, Bacterial - physiology</subject><subject>Lysophospholipase - chemistry</subject><subject>Lysophospholipase - genetics</subject><subject>Lysophospholipase - metabolism</subject><subject>Phospholipase B</subject><subject>Pseudomonas fluorescens</subject><subject>Pseudomonas fluorescens - enzymology</subject><subject>Pseudomonas fluorescens - metabolism</subject><subject>Pseudomonasfluorescens</subject><subject>Recombinant Proteins - metabolism</subject><subject>Substrate Specificity</subject><issn>0960-8524</issn><issn>1873-2976</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkcFO3DAURa2qVRlofwF5xyrh2Ukce1c6ogUJqV20a8vjvBCPEjvYCZS_r9EAW1hY3pz7rp8PIacMSgZMnO_LnQtxQTuUHBgrQZWM8Q9kw2RbFVy14iPZgBJQyIbXR-Q4pT0AVKzln8kR59BKJdSGhO0YvPO31PiO4r85YkoueBp6augteqQPbhnoPISUz-hmk5B-p8Yu7t4tj7SPYaK_E65dmII3ifbjGvIQiz5R5-llsgNGZwdnqM35L-RTb8aEX5_vE_L3x-Wf7VVx8-vn9fbiprCVUkvBGrVjgH3T7DhCJ40BsHUtGpHXsbXCnitWcWllXWHHBCjeKmmFaRgqaEV1Qs4Oc-cY7lZMi55cftQ4Go9hTVoxCUJUir-DzFUtEzKT4kDaGFKK2Os5usnER81AP1nRe_1iRT9Z0aB0tpKDp88V627C7jX2oiED3w4A5i-5dxh1sg69xc5FtIvugnur4z-htaHf</recordid><startdate>201201</startdate><enddate>201201</enddate><creator>Jiang, Fangyan</creator><creator>Huang, Shen</creator><creator>Imadad, Kaleem</creator><creator>Li, Chun</creator><general>Elsevier Ltd</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>7QO</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope></search><sort><creationdate>201201</creationdate><title>Cloning and expression of a gene with phospholipase B activity from Pseudomonas fluorescens in Escherichia coli</title><author>Jiang, Fangyan ; Huang, Shen ; Imadad, Kaleem ; Li, Chun</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c399t-159b10ef55b2e0d8aa00c44656852c49ef291328c843ed16092798c6a51e90763</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Cloning, Molecular - methods</topic><topic>Enzyme Activation</topic><topic>Enzyme Stability</topic><topic>Escherichia coli</topic><topic>Escherichia coli - enzymology</topic><topic>Escherichia coli - metabolism</topic><topic>Escherichiacoli</topic><topic>Expression</topic><topic>Gene cloning</topic><topic>Gene Expression Regulation, Bacterial - physiology</topic><topic>Lysophospholipase - chemistry</topic><topic>Lysophospholipase - genetics</topic><topic>Lysophospholipase - metabolism</topic><topic>Phospholipase B</topic><topic>Pseudomonas fluorescens</topic><topic>Pseudomonas fluorescens - enzymology</topic><topic>Pseudomonas fluorescens - metabolism</topic><topic>Pseudomonasfluorescens</topic><topic>Recombinant Proteins - metabolism</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jiang, Fangyan</creatorcontrib><creatorcontrib>Huang, Shen</creatorcontrib><creatorcontrib>Imadad, Kaleem</creatorcontrib><creatorcontrib>Li, Chun</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>Biotechnology Research Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Bioresource technology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Jiang, Fangyan</au><au>Huang, Shen</au><au>Imadad, Kaleem</au><au>Li, Chun</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cloning and expression of a gene with phospholipase B activity from Pseudomonas fluorescens in Escherichia coli</atitle><jtitle>Bioresource technology</jtitle><addtitle>Bioresour Technol</addtitle><date>2012-01</date><risdate>2012</risdate><volume>104</volume><spage>518</spage><epage>522</epage><pages>518-522</pages><issn>0960-8524</issn><eissn>1873-2976</eissn><abstract>► This is the first report on the cloning of a plb gene from the genus Pseudomonas. ► Pf-PLB from P. fluorescens BIT-18 is a member of a new phospholipase B family. ► The overproduction of Pf-PLB is of interest for the applications in many industries.
A gene from Pseudomonasfluorescens BIT-18 encoding a protein with phospholipase B activity (Pf-PLB) was cloned in E. coli BL21 (DE3). The open reading frame consists of 1272bp and potentially encodes a protein of 423 amino acid residues with a calculated molecular mass of 45.8kDa. The nucleotide sequence of Pf-PLB is 45%, 42%, 41%, 40%, 33%, and 31% identical to that of Bifidobacteriumanimals, Mycobacteriumparascrofulaceum, Acidobacteriumcapsulatum, Lactobacillusjohnsonii, Moraxellabovis, and Moraxellacatarrhalis, respectively. The His-tagged protein was purified by affinity chromatography and the eluted protein hydrolyzed both the 1- and 2-ester bond of phosphatidylcholine. The recombinant Pf-PLB had optimal activity at pH 6.0 and 30°C, and it showed 20.1% higher efficiency in the conversion rate of the phosphorus content than the wild-type.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>22078969</pmid><doi>10.1016/j.biortech.2011.09.112</doi><tpages>5</tpages></addata></record> |
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| subjects | Cloning, Molecular - methods Enzyme Activation Enzyme Stability Escherichia coli Escherichia coli - enzymology Escherichia coli - metabolism Escherichiacoli Expression Gene cloning Gene Expression Regulation, Bacterial - physiology Lysophospholipase - chemistry Lysophospholipase - genetics Lysophospholipase - metabolism Phospholipase B Pseudomonas fluorescens Pseudomonas fluorescens - enzymology Pseudomonas fluorescens - metabolism Pseudomonasfluorescens Recombinant Proteins - metabolism Substrate Specificity |
| title | Cloning and expression of a gene with phospholipase B activity from Pseudomonas fluorescens in Escherichia coli |
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