Aqueous two‐phase system based on natural quaternary ammonium compounds for the extraction of proteins
Aqueous two‐phase systems, based on the use of natural quaternary ammonium compounds, were developed to establish a benign biotechnological route for efficient protein separation. In this study, aqueous two‐phase systems of two natural resources betaine and choline with polyethyleneglycol (PEG400/60...
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| Veröffentlicht in: | Journal of separation science 2016-02, Vol.39 (4), p.648-654 |
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| creator | Zeng, Chao‐Xi Xin, Rui‐Pu Qi, Sui‐Jian Yang, Bo Wang, Yong‐Hua |
| description | Aqueous two‐phase systems, based on the use of natural quaternary ammonium compounds, were developed to establish a benign biotechnological route for efficient protein separation. In this study, aqueous two‐phase systems of two natural resources betaine and choline with polyethyleneglycol (PEG400/600) or inorganic salts (K₂HPO₄/K₃PO₄) were formed. It was shown that in the K₂HPO₄‐containing aqueous two‐phase system, hydrophobic interactions were an important driving force of protein partitioning, while protein size played a vital role in aqueous two‐phase systems that contained polyethylene glycol. An extraction efficiency of more than 90% for bovine serum albumin in the betaine/K₂HPO₄ aqueous two‐phase system can be obtained, and this betaine‐based aqueous two‐phase system provided a gentle and stable environment for the protein. In addition, after investigation of the cluster phenomenon in the betaine/K₂HPO₄ aqueous two‐phase systems, it was suggested that this phenomenon also played a significant role for protein extraction in this system. The development of aqueous two‐phase systems based on natural quaternary ammonium compounds not only provided an effective and greener method of aqueous two‐phase system to meet the requirements of green chemistry but also may help to solve the mystery of the compartmentalization of biomolecules in cells. |
| doi_str_mv | 10.1002/jssc.201500660 |
| format | Article |
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In this study, aqueous two‐phase systems of two natural resources betaine and choline with polyethyleneglycol (PEG400/600) or inorganic salts (K₂HPO₄/K₃PO₄) were formed. It was shown that in the K₂HPO₄‐containing aqueous two‐phase system, hydrophobic interactions were an important driving force of protein partitioning, while protein size played a vital role in aqueous two‐phase systems that contained polyethylene glycol. An extraction efficiency of more than 90% for bovine serum albumin in the betaine/K₂HPO₄ aqueous two‐phase system can be obtained, and this betaine‐based aqueous two‐phase system provided a gentle and stable environment for the protein. In addition, after investigation of the cluster phenomenon in the betaine/K₂HPO₄ aqueous two‐phase systems, it was suggested that this phenomenon also played a significant role for protein extraction in this system. The development of aqueous two‐phase systems based on natural quaternary ammonium compounds not only provided an effective and greener method of aqueous two‐phase system to meet the requirements of green chemistry but also may help to solve the mystery of the compartmentalization of biomolecules in cells.</description><identifier>ISSN: 1615-9306</identifier><identifier>EISSN: 1615-9314</identifier><identifier>DOI: 10.1002/jssc.201500660</identifier><identifier>PMID: 26447826</identifier><language>eng</language><publisher>Germany: Wiley-VCH</publisher><subject>Ammonium compounds ; Ammonium Compounds - chemistry ; Animals ; Aqueous two-phase systems ; betaine ; Betaine - chemistry ; Betaines ; Binary systems (materials) ; bovine serum albumin ; Cattle ; Chemical Fractionation - methods ; choline ; Choline - chemistry ; Circular Dichroism ; cluster investigation ; Dairy industry ; Extraction ; green chemistry ; Green Chemistry Technology ; Hydrophobic and Hydrophilic Interactions ; hydrophobic bonding ; Hydrophobicity ; Inorganic salts ; Light ; Macromolecular Substances - chemistry ; Muramidase - chemistry ; natural resources ; Ovalbumin - chemistry ; polyethylene glycol ; Polyethylene Glycols - chemistry ; Protein separation ; Proteins ; Proteins - chemistry ; Proteins - isolation & purification ; Quaternary ammonium compounds ; Quaternary Ammonium Compounds - chemistry ; Salts - chemistry ; Scattering, Radiation ; Separation ; Serum Albumin, Bovine - chemistry ; Trypsin - chemistry ; Water</subject><ispartof>Journal of separation science, 2016-02, Vol.39 (4), p.648-654</ispartof><rights>2015 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim</rights><rights>2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.</rights><rights>2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5661-c3b6fabbec820ec52361f51da5d5224a60785b5d22f4d0e5cca05861cd0c04193</citedby><cites>FETCH-LOGICAL-c5661-c3b6fabbec820ec52361f51da5d5224a60785b5d22f4d0e5cca05861cd0c04193</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fjssc.201500660$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fjssc.201500660$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1416,27922,27923,45572,45573</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26447826$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zeng, Chao‐Xi</creatorcontrib><creatorcontrib>Xin, Rui‐Pu</creatorcontrib><creatorcontrib>Qi, Sui‐Jian</creatorcontrib><creatorcontrib>Yang, Bo</creatorcontrib><creatorcontrib>Wang, Yong‐Hua</creatorcontrib><title>Aqueous two‐phase system based on natural quaternary ammonium compounds for the extraction of proteins</title><title>Journal of separation science</title><addtitle>J. Sep. Science</addtitle><description>Aqueous two‐phase systems, based on the use of natural quaternary ammonium compounds, were developed to establish a benign biotechnological route for efficient protein separation. In this study, aqueous two‐phase systems of two natural resources betaine and choline with polyethyleneglycol (PEG400/600) or inorganic salts (K₂HPO₄/K₃PO₄) were formed. It was shown that in the K₂HPO₄‐containing aqueous two‐phase system, hydrophobic interactions were an important driving force of protein partitioning, while protein size played a vital role in aqueous two‐phase systems that contained polyethylene glycol. An extraction efficiency of more than 90% for bovine serum albumin in the betaine/K₂HPO₄ aqueous two‐phase system can be obtained, and this betaine‐based aqueous two‐phase system provided a gentle and stable environment for the protein. In addition, after investigation of the cluster phenomenon in the betaine/K₂HPO₄ aqueous two‐phase systems, it was suggested that this phenomenon also played a significant role for protein extraction in this system. The development of aqueous two‐phase systems based on natural quaternary ammonium compounds not only provided an effective and greener method of aqueous two‐phase system to meet the requirements of green chemistry but also may help to solve the mystery of the compartmentalization of biomolecules in cells.</description><subject>Ammonium compounds</subject><subject>Ammonium Compounds - chemistry</subject><subject>Animals</subject><subject>Aqueous two-phase systems</subject><subject>betaine</subject><subject>Betaine - chemistry</subject><subject>Betaines</subject><subject>Binary systems (materials)</subject><subject>bovine serum albumin</subject><subject>Cattle</subject><subject>Chemical Fractionation - methods</subject><subject>choline</subject><subject>Choline - chemistry</subject><subject>Circular Dichroism</subject><subject>cluster investigation</subject><subject>Dairy industry</subject><subject>Extraction</subject><subject>green chemistry</subject><subject>Green Chemistry Technology</subject><subject>Hydrophobic and Hydrophilic Interactions</subject><subject>hydrophobic bonding</subject><subject>Hydrophobicity</subject><subject>Inorganic salts</subject><subject>Light</subject><subject>Macromolecular Substances - chemistry</subject><subject>Muramidase - chemistry</subject><subject>natural resources</subject><subject>Ovalbumin - chemistry</subject><subject>polyethylene glycol</subject><subject>Polyethylene Glycols - chemistry</subject><subject>Protein separation</subject><subject>Proteins</subject><subject>Proteins - chemistry</subject><subject>Proteins - isolation & purification</subject><subject>Quaternary ammonium compounds</subject><subject>Quaternary Ammonium Compounds - chemistry</subject><subject>Salts - chemistry</subject><subject>Scattering, Radiation</subject><subject>Separation</subject><subject>Serum Albumin, Bovine - chemistry</subject><subject>Trypsin - chemistry</subject><subject>Water</subject><issn>1615-9306</issn><issn>1615-9314</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkkFv1DAQhS0EoqVw5QiWuHDJMnbsSfZYVrBQFTikFUfLcRw2SxJvbUft3vgJ_EZ-CV6l7IFLT57D95417w0hLxksGAB_tw3BLDgwCYAIj8gpQyazZc7E4-MMeEKehbAFYEW5hKfkhKMQRcnxlGzObybrpkDjrfvz6_duo4OlYR-iHWid5oa6kY46Tl739GbS0fpR-z3Vw-DGbhqoccPOTWMTaOs8jRtL7V302sQuCV1Ld95F243hOXnS6j7YF_fvGbn--OFq9Sm7_Lb-vDq_zIxEZJnJa2x1XVtTcrBG8hxZK1mjZSM5FxqhKGUtG85b0YCVxmiQJTLTgAHBlvkZeTv7po_TaiGqoQvG9r0eD3sqVgJI4ALLh9ECC-T5Mj-4vvkP3bopJdHPFMiUOE_UYqaMdyF426qd74YUl2KgDnWpQ13qWFcSvLq3nerBNkf8Xz8JEDNw2_V2_4CduqiqlZCCJVk2y7pU5N1Rpv1PhUVeSPX961rxq-rLurpA9T7xr2e-1U7pH74L6rpKvphOhosSMP8LPTO6mg</recordid><startdate>201602</startdate><enddate>201602</enddate><creator>Zeng, Chao‐Xi</creator><creator>Xin, Rui‐Pu</creator><creator>Qi, Sui‐Jian</creator><creator>Yang, Bo</creator><creator>Wang, Yong‐Hua</creator><general>Wiley-VCH</general><general>Blackwell Publishing Ltd</general><general>Wiley Subscription Services, Inc</general><scope>FBQ</scope><scope>BSCLL</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>7U5</scope><scope>8FD</scope><scope>L7M</scope><scope>7X8</scope></search><sort><creationdate>201602</creationdate><title>Aqueous two‐phase system based on natural quaternary ammonium compounds for the extraction of proteins</title><author>Zeng, Chao‐Xi ; Xin, Rui‐Pu ; Qi, Sui‐Jian ; Yang, Bo ; Wang, Yong‐Hua</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5661-c3b6fabbec820ec52361f51da5d5224a60785b5d22f4d0e5cca05861cd0c04193</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Ammonium compounds</topic><topic>Ammonium Compounds - chemistry</topic><topic>Animals</topic><topic>Aqueous two-phase systems</topic><topic>betaine</topic><topic>Betaine - chemistry</topic><topic>Betaines</topic><topic>Binary systems (materials)</topic><topic>bovine serum albumin</topic><topic>Cattle</topic><topic>Chemical Fractionation - methods</topic><topic>choline</topic><topic>Choline - chemistry</topic><topic>Circular Dichroism</topic><topic>cluster investigation</topic><topic>Dairy industry</topic><topic>Extraction</topic><topic>green chemistry</topic><topic>Green Chemistry Technology</topic><topic>Hydrophobic and Hydrophilic Interactions</topic><topic>hydrophobic bonding</topic><topic>Hydrophobicity</topic><topic>Inorganic salts</topic><topic>Light</topic><topic>Macromolecular Substances - chemistry</topic><topic>Muramidase - chemistry</topic><topic>natural resources</topic><topic>Ovalbumin - chemistry</topic><topic>polyethylene glycol</topic><topic>Polyethylene Glycols - chemistry</topic><topic>Protein separation</topic><topic>Proteins</topic><topic>Proteins - chemistry</topic><topic>Proteins - isolation & purification</topic><topic>Quaternary ammonium compounds</topic><topic>Quaternary Ammonium Compounds - chemistry</topic><topic>Salts - chemistry</topic><topic>Scattering, Radiation</topic><topic>Separation</topic><topic>Serum Albumin, Bovine - chemistry</topic><topic>Trypsin - chemistry</topic><topic>Water</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zeng, Chao‐Xi</creatorcontrib><creatorcontrib>Xin, Rui‐Pu</creatorcontrib><creatorcontrib>Qi, Sui‐Jian</creatorcontrib><creatorcontrib>Yang, Bo</creatorcontrib><creatorcontrib>Wang, Yong‐Hua</creatorcontrib><collection>AGRIS</collection><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Technology Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of separation science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zeng, Chao‐Xi</au><au>Xin, Rui‐Pu</au><au>Qi, Sui‐Jian</au><au>Yang, Bo</au><au>Wang, Yong‐Hua</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Aqueous two‐phase system based on natural quaternary ammonium compounds for the extraction of proteins</atitle><jtitle>Journal of separation science</jtitle><addtitle>J. Sep. Science</addtitle><date>2016-02</date><risdate>2016</risdate><volume>39</volume><issue>4</issue><spage>648</spage><epage>654</epage><pages>648-654</pages><issn>1615-9306</issn><eissn>1615-9314</eissn><abstract>Aqueous two‐phase systems, based on the use of natural quaternary ammonium compounds, were developed to establish a benign biotechnological route for efficient protein separation. In this study, aqueous two‐phase systems of two natural resources betaine and choline with polyethyleneglycol (PEG400/600) or inorganic salts (K₂HPO₄/K₃PO₄) were formed. It was shown that in the K₂HPO₄‐containing aqueous two‐phase system, hydrophobic interactions were an important driving force of protein partitioning, while protein size played a vital role in aqueous two‐phase systems that contained polyethylene glycol. An extraction efficiency of more than 90% for bovine serum albumin in the betaine/K₂HPO₄ aqueous two‐phase system can be obtained, and this betaine‐based aqueous two‐phase system provided a gentle and stable environment for the protein. In addition, after investigation of the cluster phenomenon in the betaine/K₂HPO₄ aqueous two‐phase systems, it was suggested that this phenomenon also played a significant role for protein extraction in this system. The development of aqueous two‐phase systems based on natural quaternary ammonium compounds not only provided an effective and greener method of aqueous two‐phase system to meet the requirements of green chemistry but also may help to solve the mystery of the compartmentalization of biomolecules in cells.</abstract><cop>Germany</cop><pub>Wiley-VCH</pub><pmid>26447826</pmid><doi>10.1002/jssc.201500660</doi><tpages>7</tpages></addata></record> |
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| subjects | Ammonium compounds Ammonium Compounds - chemistry Animals Aqueous two-phase systems betaine Betaine - chemistry Betaines Binary systems (materials) bovine serum albumin Cattle Chemical Fractionation - methods choline Choline - chemistry Circular Dichroism cluster investigation Dairy industry Extraction green chemistry Green Chemistry Technology Hydrophobic and Hydrophilic Interactions hydrophobic bonding Hydrophobicity Inorganic salts Light Macromolecular Substances - chemistry Muramidase - chemistry natural resources Ovalbumin - chemistry polyethylene glycol Polyethylene Glycols - chemistry Protein separation Proteins Proteins - chemistry Proteins - isolation & purification Quaternary ammonium compounds Quaternary Ammonium Compounds - chemistry Salts - chemistry Scattering, Radiation Separation Serum Albumin, Bovine - chemistry Trypsin - chemistry Water |
| title | Aqueous two‐phase system based on natural quaternary ammonium compounds for the extraction of proteins |
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