Effective solubilization and single-step purification of Bacillus licheniformis α-amylase from insoluble aggregates
A high level expression of thermostable α-amylase gene from Bacillus licheniformis in Escherichia coli was obtained. The recombinant enzyme was mainly produced in the form of insoluble aggregates. The enzyme was solubilized without using denaturing agents and purified to homogeneity in a single step...
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| Veröffentlicht in: | Folia microbiologica 2010-03, Vol.55 (2), p.133-136 |
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| container_title | Folia microbiologica |
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| creator | Rashid, N. Ahmed, N. Saleem Haider, M. Haque, I. |
| description | A high level expression of thermostable α-amylase gene from
Bacillus licheniformis
in
Escherichia coli
was obtained. The recombinant enzyme was mainly produced in the form of insoluble aggregates. The enzyme was solubilized without using denaturing agents and purified to homogeneity in a single step by ion exchange chromatography. The enzyme was purified 138-fold with a final yield of 349 %; the specific activity of the purified enzyme was 1343 U/mg. |
| doi_str_mv | 10.1007/s12223-010-0020-y |
| format | Article |
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Bacillus licheniformis
in
Escherichia coli
was obtained. The recombinant enzyme was mainly produced in the form of insoluble aggregates. The enzyme was solubilized without using denaturing agents and purified to homogeneity in a single step by ion exchange chromatography. The enzyme was purified 138-fold with a final yield of 349 %; the specific activity of the purified enzyme was 1343 U/mg.</description><identifier>ISSN: 0015-5632</identifier><identifier>EISSN: 1874-9356</identifier><identifier>DOI: 10.1007/s12223-010-0020-y</identifier><identifier>PMID: 20490755</identifier><language>eng</language><publisher>Dordrecht: Springer Netherlands</publisher><subject>alpha-Amylases - chemistry ; alpha-Amylases - isolation & purification ; Applied Microbiology ; Bacillus - chemistry ; Bacillus - enzymology ; Bacterial Proteins - chemistry ; Bacterial Proteins - isolation & purification ; Biomedical and Life Sciences ; Chromatography, Ion Exchange - methods ; Environmental Engineering/Biotechnology ; Immunology ; Life Sciences ; Microbiology ; Solubility</subject><ispartof>Folia microbiologica, 2010-03, Vol.55 (2), p.133-136</ispartof><rights>Institute of Microbiology, v.v.i, Academy of Sciences of the Czech Republic 2010</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c343t-cd22299f232c343fd89b84efdaad44c383a80716868caa92e87a246ae77d66bf3</citedby><cites>FETCH-LOGICAL-c343t-cd22299f232c343fd89b84efdaad44c383a80716868caa92e87a246ae77d66bf3</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/s12223-010-0020-y$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s12223-010-0020-y$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20490755$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rashid, N.</creatorcontrib><creatorcontrib>Ahmed, N.</creatorcontrib><creatorcontrib>Saleem Haider, M.</creatorcontrib><creatorcontrib>Haque, I.</creatorcontrib><title>Effective solubilization and single-step purification of Bacillus licheniformis α-amylase from insoluble aggregates</title><title>Folia microbiologica</title><addtitle>Folia Microbiol</addtitle><addtitle>Folia Microbiol (Praha)</addtitle><description>A high level expression of thermostable α-amylase gene from
Bacillus licheniformis
in
Escherichia coli
was obtained. The recombinant enzyme was mainly produced in the form of insoluble aggregates. The enzyme was solubilized without using denaturing agents and purified to homogeneity in a single step by ion exchange chromatography. The enzyme was purified 138-fold with a final yield of 349 %; the specific activity of the purified enzyme was 1343 U/mg.</description><subject>alpha-Amylases - chemistry</subject><subject>alpha-Amylases - isolation & purification</subject><subject>Applied Microbiology</subject><subject>Bacillus - chemistry</subject><subject>Bacillus - enzymology</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - isolation & purification</subject><subject>Biomedical and Life Sciences</subject><subject>Chromatography, Ion Exchange - methods</subject><subject>Environmental Engineering/Biotechnology</subject><subject>Immunology</subject><subject>Life Sciences</subject><subject>Microbiology</subject><subject>Solubility</subject><issn>0015-5632</issn><issn>1874-9356</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kM1u1TAQhS0Eorc_D8AGecfKMLaTOFlCVaBSJTZlbc11xsGVE1_sBOnyVrxIn4lcUliyGmnmnKM5H2OvJLyVAOZdkUopLUCCAFAgjs_YTramEp2um-dsByBrUTdanbHzUh4AGqi0esnOFFQdmLresfnGe3Jz-EG8pLjsQww_cQ5p4jj1vIRpiCTKTAd-WHLwwW3H5PkHdCHGpfAY3Deagk95DIU__hI4HiMW4j6nkYfpT24kjsOQacCZyiV74TEWunqaF-zrx5v768_i7sun2-v3d8LpSs_C9Wu9rvNKq9PC9223byvyPWJfVU63Glswsmmb1iF2ilqDqmqQjOmbZu_1BXuz5R5y-r5Qme36oaMYcaK0FGu0ruu6M2pVyk3pciolk7eHHEbMRyvBnljbjbVdWdsTa3tcPa-f0pf9SP0_x1-4q0BtgrKepoGyfUhLntbG_0n9DWxAjdE</recordid><startdate>20100301</startdate><enddate>20100301</enddate><creator>Rashid, N.</creator><creator>Ahmed, N.</creator><creator>Saleem Haider, M.</creator><creator>Haque, I.</creator><general>Springer Netherlands</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>20100301</creationdate><title>Effective solubilization and single-step purification of Bacillus licheniformis α-amylase from insoluble aggregates</title><author>Rashid, N. ; Ahmed, N. ; Saleem Haider, M. ; Haque, I.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c343t-cd22299f232c343fd89b84efdaad44c383a80716868caa92e87a246ae77d66bf3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>alpha-Amylases - chemistry</topic><topic>alpha-Amylases - isolation & purification</topic><topic>Applied Microbiology</topic><topic>Bacillus - chemistry</topic><topic>Bacillus - enzymology</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - isolation & purification</topic><topic>Biomedical and Life Sciences</topic><topic>Chromatography, Ion Exchange - methods</topic><topic>Environmental Engineering/Biotechnology</topic><topic>Immunology</topic><topic>Life Sciences</topic><topic>Microbiology</topic><topic>Solubility</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rashid, N.</creatorcontrib><creatorcontrib>Ahmed, N.</creatorcontrib><creatorcontrib>Saleem Haider, M.</creatorcontrib><creatorcontrib>Haque, I.</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>Folia microbiologica</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rashid, N.</au><au>Ahmed, N.</au><au>Saleem Haider, M.</au><au>Haque, I.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Effective solubilization and single-step purification of Bacillus licheniformis α-amylase from insoluble aggregates</atitle><jtitle>Folia microbiologica</jtitle><stitle>Folia Microbiol</stitle><addtitle>Folia Microbiol (Praha)</addtitle><date>2010-03-01</date><risdate>2010</risdate><volume>55</volume><issue>2</issue><spage>133</spage><epage>136</epage><pages>133-136</pages><issn>0015-5632</issn><eissn>1874-9356</eissn><abstract>A high level expression of thermostable α-amylase gene from
Bacillus licheniformis
in
Escherichia coli
was obtained. The recombinant enzyme was mainly produced in the form of insoluble aggregates. The enzyme was solubilized without using denaturing agents and purified to homogeneity in a single step by ion exchange chromatography. The enzyme was purified 138-fold with a final yield of 349 %; the specific activity of the purified enzyme was 1343 U/mg.</abstract><cop>Dordrecht</cop><pub>Springer Netherlands</pub><pmid>20490755</pmid><doi>10.1007/s12223-010-0020-y</doi><tpages>4</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0015-5632 |
| ispartof | Folia microbiologica, 2010-03, Vol.55 (2), p.133-136 |
| issn | 0015-5632 1874-9356 |
| language | eng |
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| source | MEDLINE; SpringerLink Journals |
| subjects | alpha-Amylases - chemistry alpha-Amylases - isolation & purification Applied Microbiology Bacillus - chemistry Bacillus - enzymology Bacterial Proteins - chemistry Bacterial Proteins - isolation & purification Biomedical and Life Sciences Chromatography, Ion Exchange - methods Environmental Engineering/Biotechnology Immunology Life Sciences Microbiology Solubility |
| title | Effective solubilization and single-step purification of Bacillus licheniformis α-amylase from insoluble aggregates |
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