Immobilization of enzymes based on hydrophobic interaction. I. Preparation and properties of a β-amylase adsorbate
Sweet potato β‐amylase (α‐1,4 glucan maltohydrolase, EC 3.2.1.2) was immobilized through adsorption onto an agarose gel to which nonpolar side chains had been introduced via ether bridges. The adsorbent showed evidence of saturation at an enzyme content of 35 mg per milliliter of packed gel. The ads...
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| Veröffentlicht in: | Biotechnology and bioengineering 1976-11, Vol.18 (11), p.1573-1588 |
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| container_issue | 11 |
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| container_title | Biotechnology and bioengineering |
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| creator | Caldwell, Karin Dahlgren Axén, Rolf Wall, Margareta Berg Porath, Jerker |
| description | Sweet potato β‐amylase (α‐1,4 glucan maltohydrolase, EC 3.2.1.2) was immobilized through adsorption onto an agarose gel to which nonpolar side chains had been introduced via ether bridges.
The adsorbent showed evidence of saturation at an enzyme content of 35 mg per milliliter of packed gel. The adsorption was rapid and yielded a product whose operational stability depended on the initial content of β‐amylase. Activity leakage was low. The relative activity of immobilized enzyme was inversely related to the amount of enzyme adsorbed to a given gel volume, having a maximal value of around 50% at low enzyme contents. |
| doi_str_mv | 10.1002/bit.260181107 |
| format | Article |
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The adsorbent showed evidence of saturation at an enzyme content of 35 mg per milliliter of packed gel. The adsorption was rapid and yielded a product whose operational stability depended on the initial content of β‐amylase. Activity leakage was low. The relative activity of immobilized enzyme was inversely related to the amount of enzyme adsorbed to a given gel volume, having a maximal value of around 50% at low enzyme contents.</description><identifier>ISSN: 0006-3592</identifier><identifier>EISSN: 1097-0290</identifier><identifier>DOI: 10.1002/bit.260181107</identifier><identifier>PMID: 990427</identifier><language>eng</language><publisher>Hoboken: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>Adsorption ; Amylases ; Catalysis ; Enzymes, Immobilized ; Gels ; Maltose ; Polysaccharides ; Proteins - analysis ; Sepharose - analogs & derivatives ; Temperature ; Water</subject><ispartof>Biotechnology and bioengineering, 1976-11, Vol.18 (11), p.1573-1588</ispartof><rights>Copyright © 1976 John Wiley & Sons, Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c2887-8481535869c0b820c28dcfee8872b862a3c08655518f1d3f332fa1777190f1453</citedby><cites>FETCH-LOGICAL-c2887-8481535869c0b820c28dcfee8872b862a3c08655518f1d3f332fa1777190f1453</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.260181107$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fbit.260181107$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/990427$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Caldwell, Karin Dahlgren</creatorcontrib><creatorcontrib>Axén, Rolf</creatorcontrib><creatorcontrib>Wall, Margareta Berg</creatorcontrib><creatorcontrib>Porath, Jerker</creatorcontrib><title>Immobilization of enzymes based on hydrophobic interaction. I. Preparation and properties of a β-amylase adsorbate</title><title>Biotechnology and bioengineering</title><addtitle>Biotechnol. Bioeng</addtitle><description>Sweet potato β‐amylase (α‐1,4 glucan maltohydrolase, EC 3.2.1.2) was immobilized through adsorption onto an agarose gel to which nonpolar side chains had been introduced via ether bridges.
The adsorbent showed evidence of saturation at an enzyme content of 35 mg per milliliter of packed gel. The adsorption was rapid and yielded a product whose operational stability depended on the initial content of β‐amylase. Activity leakage was low. The relative activity of immobilized enzyme was inversely related to the amount of enzyme adsorbed to a given gel volume, having a maximal value of around 50% at low enzyme contents.</description><subject>Adsorption</subject><subject>Amylases</subject><subject>Catalysis</subject><subject>Enzymes, Immobilized</subject><subject>Gels</subject><subject>Maltose</subject><subject>Polysaccharides</subject><subject>Proteins - analysis</subject><subject>Sepharose - analogs & derivatives</subject><subject>Temperature</subject><subject>Water</subject><issn>0006-3592</issn><issn>1097-0290</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1976</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kLtO5DAUhi0E7A6XcjsKV3QZju2J7ZTsCNiR0EABQqKxnOREGHIZ7IyW8Fg8CM-0RhmNtqKyfP7vfDr6CfnFYMoA-Fnu-imXwDRjoHbIhEGmEuAZ7JIJAMhEpBn_SQ5CeI5fpaX8QfazDGZcTUhYNE2Xu9q92951Le0qiu370GCguQ1Y0jh7GkrfrZ4iVlDX9uht8cVO6WJKbz2urB93bVvSVSTR9y7uR5Wlnx-JbYY6qqgtQ-dz2-MR2atsHfB48x6S-8uLu_mf5PrmajE_v04KrrVK9EyzVKRaZgXkmkOclkWFGDOea8mtKEDLNE2ZrlgpKiF4ZZlSimVQsVkqDsnp6I1Hva4x9KZxocC6ti1262C0kEzNQEYwGcHCdyF4rMzKu8b6wTAwXx2b2LHZdhz5k414nTdYbumx1BirMf7rahy-d5nfi7v_xZtDXOjxbbtp_YuRSqjUPCyvjMo0W86X0jyKfxuAl10</recordid><startdate>197611</startdate><enddate>197611</enddate><creator>Caldwell, Karin Dahlgren</creator><creator>Axén, Rolf</creator><creator>Wall, Margareta Berg</creator><creator>Porath, Jerker</creator><general>Wiley Subscription Services, Inc., A Wiley Company</general><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>7X8</scope></search><sort><creationdate>197611</creationdate><title>Immobilization of enzymes based on hydrophobic interaction. I. Preparation and properties of a β-amylase adsorbate</title><author>Caldwell, Karin Dahlgren ; Axén, Rolf ; Wall, Margareta Berg ; Porath, Jerker</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c2887-8481535869c0b820c28dcfee8872b862a3c08655518f1d3f332fa1777190f1453</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1976</creationdate><topic>Adsorption</topic><topic>Amylases</topic><topic>Catalysis</topic><topic>Enzymes, Immobilized</topic><topic>Gels</topic><topic>Maltose</topic><topic>Polysaccharides</topic><topic>Proteins - analysis</topic><topic>Sepharose - analogs & derivatives</topic><topic>Temperature</topic><topic>Water</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Caldwell, Karin Dahlgren</creatorcontrib><creatorcontrib>Axén, Rolf</creatorcontrib><creatorcontrib>Wall, Margareta Berg</creatorcontrib><creatorcontrib>Porath, Jerker</creatorcontrib><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>MEDLINE - Academic</collection><jtitle>Biotechnology and bioengineering</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Caldwell, Karin Dahlgren</au><au>Axén, Rolf</au><au>Wall, Margareta Berg</au><au>Porath, Jerker</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Immobilization of enzymes based on hydrophobic interaction. I. Preparation and properties of a β-amylase adsorbate</atitle><jtitle>Biotechnology and bioengineering</jtitle><addtitle>Biotechnol. Bioeng</addtitle><date>1976-11</date><risdate>1976</risdate><volume>18</volume><issue>11</issue><spage>1573</spage><epage>1588</epage><pages>1573-1588</pages><issn>0006-3592</issn><eissn>1097-0290</eissn><abstract>Sweet potato β‐amylase (α‐1,4 glucan maltohydrolase, EC 3.2.1.2) was immobilized through adsorption onto an agarose gel to which nonpolar side chains had been introduced via ether bridges.
The adsorbent showed evidence of saturation at an enzyme content of 35 mg per milliliter of packed gel. The adsorption was rapid and yielded a product whose operational stability depended on the initial content of β‐amylase. Activity leakage was low. The relative activity of immobilized enzyme was inversely related to the amount of enzyme adsorbed to a given gel volume, having a maximal value of around 50% at low enzyme contents.</abstract><cop>Hoboken</cop><pub>Wiley Subscription Services, Inc., A Wiley Company</pub><pmid>990427</pmid><doi>10.1002/bit.260181107</doi><tpages>16</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0006-3592 |
| ispartof | Biotechnology and bioengineering, 1976-11, Vol.18 (11), p.1573-1588 |
| issn | 0006-3592 1097-0290 |
| language | eng |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete |
| subjects | Adsorption Amylases Catalysis Enzymes, Immobilized Gels Maltose Polysaccharides Proteins - analysis Sepharose - analogs & derivatives Temperature Water |
| title | Immobilization of enzymes based on hydrophobic interaction. I. Preparation and properties of a β-amylase adsorbate |
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