Immobilization of Candida rugosa lipase on modified natural wool fibers
A method has been developed to immobilize lipase from Candida rugosa on modified natural wool fibers by means of graft copolymerization of poly ethylacrylate in presence of potassium persulphate and Mohr’s salt redox initiator. The activities of free and immobilized lipase have been studied. FTIR sp...
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| Veröffentlicht in: | Reactive & functional polymers 2010-02, Vol.70 (2), p.122-128 |
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| creator | Monier, M. El-Sokkary, A.M.A. Sarhan, A.A. |
| description | A method has been developed to immobilize lipase from
Candida rugosa on modified natural wool fibers by means of graft copolymerization of poly ethylacrylate in presence of potassium persulphate and Mohr’s salt redox initiator. The activities of free and immobilized lipase have been studied. FTIR spectroscopy, scanning electron microscopy, and the Bradford method were used to characterize lipase immobilization. The efficiency of the immobilization was evaluated by examining the relative enzymatic activity of free enzyme before and after the immobilization of lipase. The results showed that the optimum temperature of immobilized lipase was 40
°C, which was identical to that of the free enzyme, and the immobilized lipase exhibited a higher relative activity than that of free lipase over 40
°C. The optimal pH for immobilized lipase was 8.0, which was higher than that of the free lipase (pH 7.5), and the immobilization resulted in stabilization of enzyme over a broader pH range. The kinetic constant value (km) of immobilized lipase was higher than that of the free lipase. However, the thermal and operational stabilities of immobilized lipase have been improved greatly. |
| doi_str_mv | 10.1016/j.reactfunctpolym.2009.11.004 |
| format | Article |
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Candida rugosa on modified natural wool fibers by means of graft copolymerization of poly ethylacrylate in presence of potassium persulphate and Mohr’s salt redox initiator. The activities of free and immobilized lipase have been studied. FTIR spectroscopy, scanning electron microscopy, and the Bradford method were used to characterize lipase immobilization. The efficiency of the immobilization was evaluated by examining the relative enzymatic activity of free enzyme before and after the immobilization of lipase. The results showed that the optimum temperature of immobilized lipase was 40
°C, which was identical to that of the free enzyme, and the immobilized lipase exhibited a higher relative activity than that of free lipase over 40
°C. The optimal pH for immobilized lipase was 8.0, which was higher than that of the free lipase (pH 7.5), and the immobilization resulted in stabilization of enzyme over a broader pH range. The kinetic constant value (km) of immobilized lipase was higher than that of the free lipase. However, the thermal and operational stabilities of immobilized lipase have been improved greatly.</description><identifier>ISSN: 1381-5148</identifier><identifier>DOI: 10.1016/j.reactfunctpolym.2009.11.004</identifier><language>eng</language><publisher>Kidlington: Elsevier B.V</publisher><subject>Applied sciences ; Biological and medical sciences ; Biotechnology ; Candida rugosa ; Enzymes ; Exact sciences and technology ; Fibers ; Fibers and threads ; Forms of application and semi-finished materials ; Fundamental and applied biological sciences. Psychology ; Grafting ; Immobilization ; Immobilization of enzymes and other molecules ; Immobilization techniques ; Lipase ; Methods. Procedures. Technologies ; Optimization ; Polymer industry, paints, wood ; Technology of polymers ; Wool</subject><ispartof>Reactive & functional polymers, 2010-02, Vol.70 (2), p.122-128</ispartof><rights>2009 Elsevier Ltd</rights><rights>2015 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c458t-28b193a89b65e7ff3bd03b344746eab22ce67124bc4c6cab34ded2fb84031c9d3</citedby><cites>FETCH-LOGICAL-c458t-28b193a89b65e7ff3bd03b344746eab22ce67124bc4c6cab34ded2fb84031c9d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.reactfunctpolym.2009.11.004$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=22371707$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Monier, M.</creatorcontrib><creatorcontrib>El-Sokkary, A.M.A.</creatorcontrib><creatorcontrib>Sarhan, A.A.</creatorcontrib><title>Immobilization of Candida rugosa lipase on modified natural wool fibers</title><title>Reactive & functional polymers</title><description>A method has been developed to immobilize lipase from
Candida rugosa on modified natural wool fibers by means of graft copolymerization of poly ethylacrylate in presence of potassium persulphate and Mohr’s salt redox initiator. The activities of free and immobilized lipase have been studied. FTIR spectroscopy, scanning electron microscopy, and the Bradford method were used to characterize lipase immobilization. The efficiency of the immobilization was evaluated by examining the relative enzymatic activity of free enzyme before and after the immobilization of lipase. The results showed that the optimum temperature of immobilized lipase was 40
°C, which was identical to that of the free enzyme, and the immobilized lipase exhibited a higher relative activity than that of free lipase over 40
°C. The optimal pH for immobilized lipase was 8.0, which was higher than that of the free lipase (pH 7.5), and the immobilization resulted in stabilization of enzyme over a broader pH range. The kinetic constant value (km) of immobilized lipase was higher than that of the free lipase. However, the thermal and operational stabilities of immobilized lipase have been improved greatly.</description><subject>Applied sciences</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Candida rugosa</subject><subject>Enzymes</subject><subject>Exact sciences and technology</subject><subject>Fibers</subject><subject>Fibers and threads</subject><subject>Forms of application and semi-finished materials</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Grafting</subject><subject>Immobilization</subject><subject>Immobilization of enzymes and other molecules</subject><subject>Immobilization techniques</subject><subject>Lipase</subject><subject>Methods. Procedures. Technologies</subject><subject>Optimization</subject><subject>Polymer industry, paints, wood</subject><subject>Technology of polymers</subject><subject>Wool</subject><issn>1381-5148</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><recordid>eNqNkTGP1DAQhVOAxHHwH9IcotngsR3HKa5AK1hOOokGamtsj5FXTrxnJ6Dj15PVnigogGqK9817o3lNcwOsAwbq3bErhG4J6-yWU06PU8cZGzuAjjH5rLkCoWHXg9Qvmpe1HhmDAZS6ag5305RtTPEnLjHPbQ7tHmcfPbZl_ZYrtimesFK7aVP2MUTy7YzLWjC1P3JObYiWSn3VPA-YKr1-mtfN148fvuw_7e4_H-727-93TvZ62XFtYRSoR6t6GkIQ1jNhhZSDVISWc0dqAC6tk0453BRPngerJRPgRi-umzcX31PJDyvVxUyxOkoJZ8prNUIJ3qte_RPkwPtRq2ED3_4V3O7VehyVOHveXlBXcq2FgjmVOGF5NMDMuQZzNH_UYM41GACz1bDt3zxFYXWYQsHZxfrbhHMxwMDOJx0uHG2f_B6pmOoizY58LOQW43P8z8Rf64eqRg</recordid><startdate>20100201</startdate><enddate>20100201</enddate><creator>Monier, M.</creator><creator>El-Sokkary, A.M.A.</creator><creator>Sarhan, A.A.</creator><general>Elsevier B.V</general><general>Elsevier</general><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7SR</scope><scope>8FD</scope><scope>JG9</scope><scope>M7N</scope></search><sort><creationdate>20100201</creationdate><title>Immobilization of Candida rugosa lipase on modified natural wool fibers</title><author>Monier, M. ; El-Sokkary, A.M.A. ; Sarhan, A.A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c458t-28b193a89b65e7ff3bd03b344746eab22ce67124bc4c6cab34ded2fb84031c9d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Applied sciences</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Candida rugosa</topic><topic>Enzymes</topic><topic>Exact sciences and technology</topic><topic>Fibers</topic><topic>Fibers and threads</topic><topic>Forms of application and semi-finished materials</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Grafting</topic><topic>Immobilization</topic><topic>Immobilization of enzymes and other molecules</topic><topic>Immobilization techniques</topic><topic>Lipase</topic><topic>Methods. Procedures. Technologies</topic><topic>Optimization</topic><topic>Polymer industry, paints, wood</topic><topic>Technology of polymers</topic><topic>Wool</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Monier, M.</creatorcontrib><creatorcontrib>El-Sokkary, A.M.A.</creatorcontrib><creatorcontrib>Sarhan, A.A.</creatorcontrib><collection>Pascal-Francis</collection><collection>CrossRef</collection><collection>Engineered Materials Abstracts</collection><collection>Technology Research Database</collection><collection>Materials Research Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><jtitle>Reactive & functional polymers</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Monier, M.</au><au>El-Sokkary, A.M.A.</au><au>Sarhan, A.A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Immobilization of Candida rugosa lipase on modified natural wool fibers</atitle><jtitle>Reactive & functional polymers</jtitle><date>2010-02-01</date><risdate>2010</risdate><volume>70</volume><issue>2</issue><spage>122</spage><epage>128</epage><pages>122-128</pages><issn>1381-5148</issn><abstract>A method has been developed to immobilize lipase from
Candida rugosa on modified natural wool fibers by means of graft copolymerization of poly ethylacrylate in presence of potassium persulphate and Mohr’s salt redox initiator. The activities of free and immobilized lipase have been studied. FTIR spectroscopy, scanning electron microscopy, and the Bradford method were used to characterize lipase immobilization. The efficiency of the immobilization was evaluated by examining the relative enzymatic activity of free enzyme before and after the immobilization of lipase. The results showed that the optimum temperature of immobilized lipase was 40
°C, which was identical to that of the free enzyme, and the immobilized lipase exhibited a higher relative activity than that of free lipase over 40
°C. The optimal pH for immobilized lipase was 8.0, which was higher than that of the free lipase (pH 7.5), and the immobilization resulted in stabilization of enzyme over a broader pH range. The kinetic constant value (km) of immobilized lipase was higher than that of the free lipase. However, the thermal and operational stabilities of immobilized lipase have been improved greatly.</abstract><cop>Kidlington</cop><pub>Elsevier B.V</pub><doi>10.1016/j.reactfunctpolym.2009.11.004</doi><tpages>7</tpages></addata></record> |
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| subjects | Applied sciences Biological and medical sciences Biotechnology Candida rugosa Enzymes Exact sciences and technology Fibers Fibers and threads Forms of application and semi-finished materials Fundamental and applied biological sciences. Psychology Grafting Immobilization Immobilization of enzymes and other molecules Immobilization techniques Lipase Methods. Procedures. Technologies Optimization Polymer industry, paints, wood Technology of polymers Wool |
| title | Immobilization of Candida rugosa lipase on modified natural wool fibers |
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