Interaction of invertase with polyelectrolytes
In connection with our work on polyelectrolyte complex formation with polyampholytes, the interaction between invertase and several linear polyelectorlytes has been investigated by means of turbidimetry, light scattering measurements, and determination of the enzyme activity. Polyelectrolyte complex...
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Veröffentlicht in: | Biotechnology and bioengineering 1991-11, Vol.38 (9), p.1012-1019 |
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creator | Dautzenberg, Herbert Kötz, Joachim Philipp, Burkart Rother, Gudrun Schellenberger, Alfred Mansfeld, Johanna |
description | In connection with our work on polyelectrolyte complex formation with polyampholytes, the interaction between invertase and several linear polyelectorlytes has been investigated by means of turbidimetry, light scattering measurements, and determination of the enzyme activity. Polyelectrolyte complex formation of invertase was shown to occur with cationic polyelectrolytes only. The light‐scattering data yield information on aggregation and desegregation processes in complex formation. As indicated by our results, only a part of the protein molecules is engaged in this Coulombic interaction, and this part shows a rather small enzyme activity only. Thus, a direct interaction between invertase and a cationic polyelectrolyte is no effective approach to enzyme binding, but a complete immobilization of invertase can be achieved via an “inclusion flocculation” with a symplex formed by interaction between an anionic and a cationic linear polyelectrolyte or via immobilization in symplex microcapsules. |
doi_str_mv | 10.1002/bit.260380909 |
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Polyelectrolyte complex formation of invertase was shown to occur with cationic polyelectrolytes only. The light‐scattering data yield information on aggregation and desegregation processes in complex formation. As indicated by our results, only a part of the protein molecules is engaged in this Coulombic interaction, and this part shows a rather small enzyme activity only. Thus, a direct interaction between invertase and a cationic polyelectrolyte is no effective approach to enzyme binding, but a complete immobilization of invertase can be achieved via an “inclusion flocculation” with a symplex formed by interaction between an anionic and a cationic linear polyelectrolyte or via immobilization in symplex microcapsules.</description><identifier>ISSN: 0006-3592</identifier><identifier>EISSN: 1097-0290</identifier><identifier>DOI: 10.1002/bit.260380909</identifier><identifier>PMID: 18600865</identifier><identifier>CODEN: BIBIAU</identifier><language>eng</language><publisher>Hoboken: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>beta -fructofuranosidase ; Biological and medical sciences ; electrolytes ; Fundamental and applied biological sciences. Psychology ; interaction ; Interactions. Associations ; Intermolecular phenomena ; invertase ; ions ; Molecular biophysics ; polyampholytes ; polyelectrolytes ; Saccharomyces cerevisiae</subject><ispartof>Biotechnology and bioengineering, 1991-11, Vol.38 (9), p.1012-1019</ispartof><rights>Copyright © 1991 John Wiley & Sons, Inc.</rights><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4729-ac20df0b8c9effe44f267554723e5a41ed568428ee6bd3e609584146df3b5993</citedby><cites>FETCH-LOGICAL-c4729-ac20df0b8c9effe44f267554723e5a41ed568428ee6bd3e609584146df3b5993</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%2Fbit.260380909$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fbit.260380909$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,27924,27925,45574,45575</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5129152$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18600865$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Dautzenberg, Herbert</creatorcontrib><creatorcontrib>Kötz, Joachim</creatorcontrib><creatorcontrib>Philipp, Burkart</creatorcontrib><creatorcontrib>Rother, Gudrun</creatorcontrib><creatorcontrib>Schellenberger, Alfred</creatorcontrib><creatorcontrib>Mansfeld, Johanna</creatorcontrib><title>Interaction of invertase with polyelectrolytes</title><title>Biotechnology and bioengineering</title><addtitle>Biotechnol. Bioeng</addtitle><description>In connection with our work on polyelectrolyte complex formation with polyampholytes, the interaction between invertase and several linear polyelectorlytes has been investigated by means of turbidimetry, light scattering measurements, and determination of the enzyme activity. Polyelectrolyte complex formation of invertase was shown to occur with cationic polyelectrolytes only. The light‐scattering data yield information on aggregation and desegregation processes in complex formation. As indicated by our results, only a part of the protein molecules is engaged in this Coulombic interaction, and this part shows a rather small enzyme activity only. Thus, a direct interaction between invertase and a cationic polyelectrolyte is no effective approach to enzyme binding, but a complete immobilization of invertase can be achieved via an “inclusion flocculation” with a symplex formed by interaction between an anionic and a cationic linear polyelectrolyte or via immobilization in symplex microcapsules.</description><subject>beta -fructofuranosidase</subject><subject>Biological and medical sciences</subject><subject>electrolytes</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>interaction</subject><subject>Interactions. Associations</subject><subject>Intermolecular phenomena</subject><subject>invertase</subject><subject>ions</subject><subject>Molecular biophysics</subject><subject>polyampholytes</subject><subject>polyelectrolytes</subject><subject>Saccharomyces cerevisiae</subject><issn>0006-3592</issn><issn>1097-0290</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><recordid>eNp90E1vEzEQBmALgWhaOHJFOSA4bRh_20daaIlUARKROFpe71gYNrvB3lDy72uUVeDUk8fyM-PRS8gLCisKwN62aVoxBdyABfuILChY3QCz8JgsAEA1XFp2Rs5L-VGv2ij1lJxRowCMkguyWg8TZh-mNA7LMS7T8Bvz5Asu79L0fbkb-wP2GKZciwnLM_Ik-r7g8_m8IJvrD5urj83t55v11bvbJgjNbOMDgy5Ca4LFGFGIyJSWsr5xlF5Q7KQyghlE1XYcFVhpBBWqi7yV1vIL8uY4dpfHX3ssk9umErDv_YDjvjjNuVJUGVnl6wclVUwKpUWFzRGGPJaSMbpdTlufD46C-5ukq0m6U5LVv5wH79stdv_0HF0Fr2bgS_B9zH4IqZycpMxSySrTR3aXejw8_Km7XG_-32DeOJUJ_5w6ff7plOZaum-fbtyXjf0q2Xvjrvk9eaiZtQ</recordid><startdate>199111</startdate><enddate>199111</enddate><creator>Dautzenberg, Herbert</creator><creator>Kötz, Joachim</creator><creator>Philipp, Burkart</creator><creator>Rother, Gudrun</creator><creator>Schellenberger, Alfred</creator><creator>Mansfeld, Johanna</creator><general>Wiley Subscription Services, Inc., A Wiley Company</general><general>Wiley</general><scope>BSCLL</scope><scope>IQODW</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M7N</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>199111</creationdate><title>Interaction of invertase with polyelectrolytes</title><author>Dautzenberg, Herbert ; Kötz, Joachim ; Philipp, Burkart ; Rother, Gudrun ; Schellenberger, Alfred ; Mansfeld, Johanna</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4729-ac20df0b8c9effe44f267554723e5a41ed568428ee6bd3e609584146df3b5993</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>beta -fructofuranosidase</topic><topic>Biological and medical sciences</topic><topic>electrolytes</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>interaction</topic><topic>Interactions. Associations</topic><topic>Intermolecular phenomena</topic><topic>invertase</topic><topic>ions</topic><topic>Molecular biophysics</topic><topic>polyampholytes</topic><topic>polyelectrolytes</topic><topic>Saccharomyces cerevisiae</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Dautzenberg, Herbert</creatorcontrib><creatorcontrib>Kötz, Joachim</creatorcontrib><creatorcontrib>Philipp, Burkart</creatorcontrib><creatorcontrib>Rother, Gudrun</creatorcontrib><creatorcontrib>Schellenberger, Alfred</creatorcontrib><creatorcontrib>Mansfeld, Johanna</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biotechnology and bioengineering</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Dautzenberg, Herbert</au><au>Kötz, Joachim</au><au>Philipp, Burkart</au><au>Rother, Gudrun</au><au>Schellenberger, Alfred</au><au>Mansfeld, Johanna</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Interaction of invertase with polyelectrolytes</atitle><jtitle>Biotechnology and bioengineering</jtitle><addtitle>Biotechnol. Bioeng</addtitle><date>1991-11</date><risdate>1991</risdate><volume>38</volume><issue>9</issue><spage>1012</spage><epage>1019</epage><pages>1012-1019</pages><issn>0006-3592</issn><eissn>1097-0290</eissn><coden>BIBIAU</coden><abstract>In connection with our work on polyelectrolyte complex formation with polyampholytes, the interaction between invertase and several linear polyelectorlytes has been investigated by means of turbidimetry, light scattering measurements, and determination of the enzyme activity. Polyelectrolyte complex formation of invertase was shown to occur with cationic polyelectrolytes only. The light‐scattering data yield information on aggregation and desegregation processes in complex formation. As indicated by our results, only a part of the protein molecules is engaged in this Coulombic interaction, and this part shows a rather small enzyme activity only. Thus, a direct interaction between invertase and a cationic polyelectrolyte is no effective approach to enzyme binding, but a complete immobilization of invertase can be achieved via an “inclusion flocculation” with a symplex formed by interaction between an anionic and a cationic linear polyelectrolyte or via immobilization in symplex microcapsules.</abstract><cop>Hoboken</cop><pub>Wiley Subscription Services, Inc., A Wiley Company</pub><pmid>18600865</pmid><doi>10.1002/bit.260380909</doi><tpages>8</tpages></addata></record> |
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subjects | beta -fructofuranosidase Biological and medical sciences electrolytes Fundamental and applied biological sciences. Psychology interaction Interactions. Associations Intermolecular phenomena invertase ions Molecular biophysics polyampholytes polyelectrolytes Saccharomyces cerevisiae |
title | Interaction of invertase with polyelectrolytes |
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