Enhancement of the thermal and storage stability of urease by covalent attachment to phospholipid-bound silica
Urease was immobilized directly on silanized silica surfaces carrying alkyl moieties with terminal carboxylic groups. The enzyme was also covalently attached to phospholipid-bound silanized silica surfaces through the terminal carboxyl moiety on the sn-2 acyl chain of the lipid. The surfaces were ch...
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| Veröffentlicht in: | Analytical chemistry (Washington) 1992-05, Vol.64 (9), p.1062-1068 |
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| container_title | Analytical chemistry (Washington) |
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| creator | Kallury, Krishna M. R Lee, William E Thompson, Michael |
| description | Urease was immobilized directly on silanized silica surfaces carrying alkyl moieties with terminal carboxylic groups. The enzyme was also covalently attached to phospholipid-bound silanized silica surfaces through the terminal carboxyl moiety on the sn-2 acyl chain of the lipid. The surfaces were characterized by X-ray photoelectron spectroscopy and ellipsometry. The activity of the immobilized urease was determined by UV spectrophotometry using a urea/bromocresol purple substrate. The enzymic activity decreases exponentially upon storage under dry solid conditions for 1 week or upon heating to 100 degrees C in the case of the silane/enzyme surfaces. On the other hand, the enzyme immobilized on phospholipid-carrying silica surfaces retained its entire original activity under dry storage or heat treatment conditions. Such immobilized urease systems could find extensive applicability in the design of in vivo dialysis equipment or for on-line monitoring of urea. |
| doi_str_mv | 10.1021/ac00033a018 |
| format | Article |
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R ; Lee, William E ; Thompson, Michael</creator><creatorcontrib>Kallury, Krishna M. R ; Lee, William E ; Thompson, Michael</creatorcontrib><description>Urease was immobilized directly on silanized silica surfaces carrying alkyl moieties with terminal carboxylic groups. The enzyme was also covalently attached to phospholipid-bound silanized silica surfaces through the terminal carboxyl moiety on the sn-2 acyl chain of the lipid. The surfaces were characterized by X-ray photoelectron spectroscopy and ellipsometry. The activity of the immobilized urease was determined by UV spectrophotometry using a urea/bromocresol purple substrate. The enzymic activity decreases exponentially upon storage under dry solid conditions for 1 week or upon heating to 100 degrees C in the case of the silane/enzyme surfaces. On the other hand, the enzyme immobilized on phospholipid-carrying silica surfaces retained its entire original activity under dry storage or heat treatment conditions. Such immobilized urease systems could find extensive applicability in the design of in vivo dialysis equipment or for on-line monitoring of urea.</description><identifier>ISSN: 0003-2700</identifier><identifier>EISSN: 1520-6882</identifier><identifier>DOI: 10.1021/ac00033a018</identifier><identifier>PMID: 1317138</identifier><identifier>CODEN: ANCHAM</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Biological and medical sciences ; Biosensors ; Biotechnology ; Enzyme Stability ; Enzymes, Immobilized ; Fundamental and applied biological sciences. Psychology ; Hot Temperature ; Methods. Procedures. 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R</creatorcontrib><creatorcontrib>Lee, William E</creatorcontrib><creatorcontrib>Thompson, Michael</creatorcontrib><title>Enhancement of the thermal and storage stability of urease by covalent attachment to phospholipid-bound silica</title><title>Analytical chemistry (Washington)</title><addtitle>Anal. Chem</addtitle><description>Urease was immobilized directly on silanized silica surfaces carrying alkyl moieties with terminal carboxylic groups. The enzyme was also covalently attached to phospholipid-bound silanized silica surfaces through the terminal carboxyl moiety on the sn-2 acyl chain of the lipid. The surfaces were characterized by X-ray photoelectron spectroscopy and ellipsometry. The activity of the immobilized urease was determined by UV spectrophotometry using a urea/bromocresol purple substrate. The enzymic activity decreases exponentially upon storage under dry solid conditions for 1 week or upon heating to 100 degrees C in the case of the silane/enzyme surfaces. On the other hand, the enzyme immobilized on phospholipid-carrying silica surfaces retained its entire original activity under dry storage or heat treatment conditions. Such immobilized urease systems could find extensive applicability in the design of in vivo dialysis equipment or for on-line monitoring of urea.</description><subject>Biological and medical sciences</subject><subject>Biosensors</subject><subject>Biotechnology</subject><subject>Enzyme Stability</subject><subject>Enzymes, Immobilized</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hot Temperature</subject><subject>Methods. Procedures. Technologies</subject><subject>Phospholipids</subject><subject>Silicon Dioxide</subject><subject>Spectrophotometry</subject><subject>Urease - chemistry</subject><subject>Various methods and equipments</subject><issn>0003-2700</issn><issn>1520-6882</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkE1v1DAQhi0EKkvhxBkpBwQHFBjbiT-OaFUKaCWKWs7WxHHYlCTe2g5i_z0OWRUOHEYj-X3mlfUQ8pzCWwqMvkMLAJwjUPWAbGjNoBRKsYdks7yXTAI8Jk9ivAWgFKg4I2eUU0m52pDpYtrjZN3oplT4rkh7t0wYcShwaouYfMDvLm9s-qFPxwWag8PoiuZYWP8Th-UUU0K7_9OSfHHY-5hn6A99WzZ-XorytcWn5FGHQ3TPTvucfPtwcbP9WO6-XH7avt-VWFGdyrpRbadYIzVvHKNaVNpVWnKNtAFmaw4CRMuc1G0naqhoV4HlVnFZCQDb8XPyau09BH83u5jM2EfrhgEn5-doJNMCpBAZfLOCNvgYg-vMIfQjhqOhYBa75h-7mX5xqp2b0bV_2VVnzl-ecowWhy5ktX28x2qmldI0Y-WK9TG5X_cxhh9GSC5rc3N1bS613H7eXV-Zr5l_vfJoo7n1c5iyu_9-8DeZip1T</recordid><startdate>19920501</startdate><enddate>19920501</enddate><creator>Kallury, Krishna M. R</creator><creator>Lee, William E</creator><creator>Thompson, Michael</creator><general>American Chemical Society</general><scope>BSCLL</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>19920501</creationdate><title>Enhancement of the thermal and storage stability of urease by covalent attachment to phospholipid-bound silica</title><author>Kallury, Krishna M. R ; Lee, William E ; Thompson, Michael</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a419t-5b8df82b793be219649e49739a1b02c530606d2e79df65041f40c3c8374600cf3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Biological and medical sciences</topic><topic>Biosensors</topic><topic>Biotechnology</topic><topic>Enzyme Stability</topic><topic>Enzymes, Immobilized</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hot Temperature</topic><topic>Methods. Procedures. Technologies</topic><topic>Phospholipids</topic><topic>Silicon Dioxide</topic><topic>Spectrophotometry</topic><topic>Urease - chemistry</topic><topic>Various methods and equipments</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kallury, Krishna M. R</creatorcontrib><creatorcontrib>Lee, William E</creatorcontrib><creatorcontrib>Thompson, Michael</creatorcontrib><collection>Istex</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>Analytical chemistry (Washington)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kallury, Krishna M. R</au><au>Lee, William E</au><au>Thompson, Michael</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Enhancement of the thermal and storage stability of urease by covalent attachment to phospholipid-bound silica</atitle><jtitle>Analytical chemistry (Washington)</jtitle><addtitle>Anal. Chem</addtitle><date>1992-05-01</date><risdate>1992</risdate><volume>64</volume><issue>9</issue><spage>1062</spage><epage>1068</epage><pages>1062-1068</pages><issn>0003-2700</issn><eissn>1520-6882</eissn><coden>ANCHAM</coden><abstract>Urease was immobilized directly on silanized silica surfaces carrying alkyl moieties with terminal carboxylic groups. The enzyme was also covalently attached to phospholipid-bound silanized silica surfaces through the terminal carboxyl moiety on the sn-2 acyl chain of the lipid. The surfaces were characterized by X-ray photoelectron spectroscopy and ellipsometry. The activity of the immobilized urease was determined by UV spectrophotometry using a urea/bromocresol purple substrate. The enzymic activity decreases exponentially upon storage under dry solid conditions for 1 week or upon heating to 100 degrees C in the case of the silane/enzyme surfaces. On the other hand, the enzyme immobilized on phospholipid-carrying silica surfaces retained its entire original activity under dry storage or heat treatment conditions. Such immobilized urease systems could find extensive applicability in the design of in vivo dialysis equipment or for on-line monitoring of urea.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>1317138</pmid><doi>10.1021/ac00033a018</doi><tpages>7</tpages></addata></record> |
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| ispartof | Analytical chemistry (Washington), 1992-05, Vol.64 (9), p.1062-1068 |
| issn | 0003-2700 1520-6882 |
| language | eng |
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| source | MEDLINE; ACS Publications |
| subjects | Biological and medical sciences Biosensors Biotechnology Enzyme Stability Enzymes, Immobilized Fundamental and applied biological sciences. Psychology Hot Temperature Methods. Procedures. Technologies Phospholipids Silicon Dioxide Spectrophotometry Urease - chemistry Various methods and equipments |
| title | Enhancement of the thermal and storage stability of urease by covalent attachment to phospholipid-bound silica |
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