Transgenic Soybean Seed as Protein Expression System: Aqueous Extraction of Recombinant β-Glucuronidase
Soybean is one of the plant species with potential to be used as seed-based bioreactor. As part of the downstream processing (DSP) of this technology, extraction is a key step, since it defines the composition of the solution from which the recombinant product will be purified. In the present work,...
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| Veröffentlicht in: | Applied biochemistry and biotechnology 2010-02, Vol.160 (4), p.1157-1167 |
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| container_title | Applied biochemistry and biotechnology |
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| creator | Robić, Goran Farinas, Cristiane S Rech, Elíbio L Miranda, Everson A |
| description | Soybean is one of the plant species with potential to be used as seed-based bioreactor. As part of the downstream processing (DSP) of this technology, extraction is a key step, since it defines the composition of the solution from which the recombinant product will be purified. In the present work, the characteristics of soybean seeds used as a bioreactor were evaluated from a process engineering standpoint through analysis of the influence of pH and ionic strength on the extraction of recombinant β-glucuronidase (rGUS). Concentrations of recombinant protein and native soybean compounds were analyzed and compared with similar data from extraction studies using transgenic corn seeds as bioreactor. Efficient rGUS extraction was obtained at pH of around 5.5 with no addition of salt. Soybean seed extracts had lower levels of co-extracted native compounds, than corn seed extracts, and should be considered as a potential plant bioreactor in terms of DSP. |
| doi_str_mv | 10.1007/s12010-009-8637-5 |
| format | Article |
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Soybean seed extracts had lower levels of co-extracted native compounds, than corn seed extracts, and should be considered as a potential plant bioreactor in terms of DSP.</description><identifier>ISSN: 0273-2289</identifier><identifier>EISSN: 1559-0291</identifier><identifier>DOI: 10.1007/s12010-009-8637-5</identifier><identifier>PMID: 19412577</identifier><identifier>CODEN: ABIBDL</identifier><language>eng</language><publisher>New York: New York : Humana Press Inc</publisher><subject>beta-glucuronidase ; Biochemistry ; Biological and medical sciences ; Bioreactors ; Biotechnology ; Chemistry ; Chemistry and Materials Science ; extraction ; Fundamental and applied biological sciences. Psychology ; Gene Expression Regulation, Plant ; Glucuronidase - biosynthesis ; Glucuronidase - genetics ; Glucuronidase - isolation & purification ; Glycine max ; Glycine max - genetics ; Hydrogen-Ion Concentration ; ionic strength ; Plant Proteins - biosynthesis ; Plant Proteins - genetics ; Plants, Genetically Modified - genetics ; recombinant proteins ; Recombinant Proteins - biosynthesis ; seeds ; Seeds - genetics ; soybeans ; transgenic plants ; Zea mays - genetics</subject><ispartof>Applied biochemistry and biotechnology, 2010-02, Vol.160 (4), p.1157-1167</ispartof><rights>Humana Press 2009</rights><rights>2015 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c440t-b3971f34fe9e799c6945f4708160de69412c0c904ab7b8903fb99d5dae30bf7a3</citedby><cites>FETCH-LOGICAL-c440t-b3971f34fe9e799c6945f4708160de69412c0c904ab7b8903fb99d5dae30bf7a3</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/s12010-009-8637-5$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s12010-009-8637-5$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=22773278$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19412577$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Robić, Goran</creatorcontrib><creatorcontrib>Farinas, Cristiane S</creatorcontrib><creatorcontrib>Rech, Elíbio L</creatorcontrib><creatorcontrib>Miranda, Everson A</creatorcontrib><title>Transgenic Soybean Seed as Protein Expression System: Aqueous Extraction of Recombinant β-Glucuronidase</title><title>Applied biochemistry and biotechnology</title><addtitle>Appl Biochem Biotechnol</addtitle><addtitle>Appl Biochem Biotechnol</addtitle><description>Soybean is one of the plant species with potential to be used as seed-based bioreactor. As part of the downstream processing (DSP) of this technology, extraction is a key step, since it defines the composition of the solution from which the recombinant product will be purified. In the present work, the characteristics of soybean seeds used as a bioreactor were evaluated from a process engineering standpoint through analysis of the influence of pH and ionic strength on the extraction of recombinant β-glucuronidase (rGUS). Concentrations of recombinant protein and native soybean compounds were analyzed and compared with similar data from extraction studies using transgenic corn seeds as bioreactor. Efficient rGUS extraction was obtained at pH of around 5.5 with no addition of salt. Soybean seed extracts had lower levels of co-extracted native compounds, than corn seed extracts, and should be considered as a potential plant bioreactor in terms of DSP.</description><subject>beta-glucuronidase</subject><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Bioreactors</subject><subject>Biotechnology</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>extraction</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Expression Regulation, Plant</subject><subject>Glucuronidase - biosynthesis</subject><subject>Glucuronidase - genetics</subject><subject>Glucuronidase - isolation & purification</subject><subject>Glycine max</subject><subject>Glycine max - genetics</subject><subject>Hydrogen-Ion Concentration</subject><subject>ionic strength</subject><subject>Plant Proteins - biosynthesis</subject><subject>Plant Proteins - genetics</subject><subject>Plants, Genetically Modified - genetics</subject><subject>recombinant proteins</subject><subject>Recombinant Proteins - biosynthesis</subject><subject>seeds</subject><subject>Seeds - genetics</subject><subject>soybeans</subject><subject>transgenic plants</subject><subject>Zea mays - genetics</subject><issn>0273-2289</issn><issn>1559-0291</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kMFu1DAQhi0EotvCA3CBXFBPgbGdrGNuVVUKUiUQ254txxkvqRJ78SQS-1o8CM-Eo6zgxsmH__vHMx9jrzi84wDqPXEBHEoAXTZbqcr6CdvwutYlCM2fsg0IJUshGn3GzokeAbhoavWcnXFdcVErtWHf75MNtMfQu2IXjy3aUOwQu8JS8TXFCftQ3Pw8JCTqY46ONOH4obj6MWOcKUdTsm5aouiLb-ji2PbBhqn4_au8HWY3pxj6zhK-YM-8HQhfnt4L9vDx5v76U3n35fbz9dVd6aoKprKVWnEvK48aldZuq6vaVwoavoUOt8veDpyGyraqbTRI32rd1Z1FCa1XVl6wy3XuIcW8JE1m7MnhMNiwbGyUlFooXulM8pV0KRIl9OaQ-tGmo-FgFr9m9WuyX7P4NXXuvD5Nn9sRu3-Nk9AMvD0BlpwdfLbrevrLCZEZoZrMiZWjHIU9JvMY5xSymf_-_mYteRuN3ac8-GGXIQm8yVg-7Q9Rup00</recordid><startdate>20100201</startdate><enddate>20100201</enddate><creator>Robić, Goran</creator><creator>Farinas, Cristiane S</creator><creator>Rech, Elíbio L</creator><creator>Miranda, Everson A</creator><general>New York : Humana Press Inc</general><general>Humana Press Inc</general><general>Springer</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>7X8</scope></search><sort><creationdate>20100201</creationdate><title>Transgenic Soybean Seed as Protein Expression System: Aqueous Extraction of Recombinant β-Glucuronidase</title><author>Robić, Goran ; Farinas, Cristiane S ; Rech, Elíbio L ; Miranda, Everson A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c440t-b3971f34fe9e799c6945f4708160de69412c0c904ab7b8903fb99d5dae30bf7a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>beta-glucuronidase</topic><topic>Biochemistry</topic><topic>Biological and medical sciences</topic><topic>Bioreactors</topic><topic>Biotechnology</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>extraction</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Expression Regulation, Plant</topic><topic>Glucuronidase - biosynthesis</topic><topic>Glucuronidase - genetics</topic><topic>Glucuronidase - isolation & purification</topic><topic>Glycine max</topic><topic>Glycine max - genetics</topic><topic>Hydrogen-Ion Concentration</topic><topic>ionic strength</topic><topic>Plant Proteins - biosynthesis</topic><topic>Plant Proteins - genetics</topic><topic>Plants, Genetically Modified - genetics</topic><topic>recombinant proteins</topic><topic>Recombinant Proteins - biosynthesis</topic><topic>seeds</topic><topic>Seeds - genetics</topic><topic>soybeans</topic><topic>transgenic plants</topic><topic>Zea mays - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Robić, Goran</creatorcontrib><creatorcontrib>Farinas, Cristiane S</creatorcontrib><creatorcontrib>Rech, Elíbio L</creatorcontrib><creatorcontrib>Miranda, Everson A</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>MEDLINE - Academic</collection><jtitle>Applied biochemistry and biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Robić, Goran</au><au>Farinas, Cristiane S</au><au>Rech, Elíbio L</au><au>Miranda, Everson A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Transgenic Soybean Seed as Protein Expression System: Aqueous Extraction of Recombinant β-Glucuronidase</atitle><jtitle>Applied biochemistry and biotechnology</jtitle><stitle>Appl Biochem Biotechnol</stitle><addtitle>Appl Biochem Biotechnol</addtitle><date>2010-02-01</date><risdate>2010</risdate><volume>160</volume><issue>4</issue><spage>1157</spage><epage>1167</epage><pages>1157-1167</pages><issn>0273-2289</issn><eissn>1559-0291</eissn><coden>ABIBDL</coden><abstract>Soybean is one of the plant species with potential to be used as seed-based bioreactor. As part of the downstream processing (DSP) of this technology, extraction is a key step, since it defines the composition of the solution from which the recombinant product will be purified. In the present work, the characteristics of soybean seeds used as a bioreactor were evaluated from a process engineering standpoint through analysis of the influence of pH and ionic strength on the extraction of recombinant β-glucuronidase (rGUS). Concentrations of recombinant protein and native soybean compounds were analyzed and compared with similar data from extraction studies using transgenic corn seeds as bioreactor. Efficient rGUS extraction was obtained at pH of around 5.5 with no addition of salt. 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| subjects | beta-glucuronidase Biochemistry Biological and medical sciences Bioreactors Biotechnology Chemistry Chemistry and Materials Science extraction Fundamental and applied biological sciences. Psychology Gene Expression Regulation, Plant Glucuronidase - biosynthesis Glucuronidase - genetics Glucuronidase - isolation & purification Glycine max Glycine max - genetics Hydrogen-Ion Concentration ionic strength Plant Proteins - biosynthesis Plant Proteins - genetics Plants, Genetically Modified - genetics recombinant proteins Recombinant Proteins - biosynthesis seeds Seeds - genetics soybeans transgenic plants Zea mays - genetics |
| title | Transgenic Soybean Seed as Protein Expression System: Aqueous Extraction of Recombinant β-Glucuronidase |
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