Bioactive polymers. 56: Urease immobilization on carboxymethylcellulose
This article reports on the reaction of urease immobilization through its covalent bonding on carboxymethylcellulose. The reaction is activated by dicyclohexylcarbodiimide. The coupling reaction is influenced by the enzyme–support and activator–support ratios, as well as by duration. Starting from a...
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| Veröffentlicht in: | Biotechnology and bioengineering 1989-07, Vol.34 (3), p.283-290 |
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| container_title | Biotechnology and bioengineering |
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| creator | Dumitriu, Severian Popa, Marcel Artenie, Vlad Dan, Florin |
| description | This article reports on the reaction of urease immobilization through its covalent bonding on carboxymethylcellulose. The reaction is activated by dicyclohexylcarbodiimide. The coupling reaction is influenced by the enzyme–support and activator–support ratios, as well as by duration. Starting from a rotating, composed experimental program of the second order, the function correlating the activity of the immobilized enzyme with the reaction parameters is established. Immobilized urease exhibits thermal stability higher than that of free enzyme, regarding both pH and the inhibiting action of some metal ions or organic substances. The stability over time of the immobilized urease is high, its enzymatic activity being maintained at over 85% of the initial value three months after synthesis. |
| doi_str_mv | 10.1002/bit.260340302 |
| format | Article |
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The reaction is activated by dicyclohexylcarbodiimide. The coupling reaction is influenced by the enzyme–support and activator–support ratios, as well as by duration. Starting from a rotating, composed experimental program of the second order, the function correlating the activity of the immobilized enzyme with the reaction parameters is established. Immobilized urease exhibits thermal stability higher than that of free enzyme, regarding both pH and the inhibiting action of some metal ions or organic substances. The stability over time of the immobilized urease is high, its enzymatic activity being maintained at over 85% of the initial value three months after synthesis.</description><identifier>ISSN: 0006-3592</identifier><identifier>EISSN: 1097-0290</identifier><identifier>DOI: 10.1002/bit.260340302</identifier><identifier>PMID: 18588105</identifier><identifier>CODEN: BIBIAU</identifier><language>eng</language><publisher>Hoboken: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>Biological and medical sciences ; Biotechnology ; dicyclohexylcarbodiimide ; Enzyme engineering ; Fundamental and applied biological sciences. Psychology ; Immobilization of enzymes and other molecules ; Immobilization techniques ; immobilized enzymes ; Methods. Procedures. 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Bioeng</addtitle><description>This article reports on the reaction of urease immobilization through its covalent bonding on carboxymethylcellulose. The reaction is activated by dicyclohexylcarbodiimide. The coupling reaction is influenced by the enzyme–support and activator–support ratios, as well as by duration. Starting from a rotating, composed experimental program of the second order, the function correlating the activity of the immobilized enzyme with the reaction parameters is established. Immobilized urease exhibits thermal stability higher than that of free enzyme, regarding both pH and the inhibiting action of some metal ions or organic substances. The stability over time of the immobilized urease is high, its enzymatic activity being maintained at over 85% of the initial value three months after synthesis.</description><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>dicyclohexylcarbodiimide</subject><subject>Enzyme engineering</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Immobilization of enzymes and other molecules</subject><subject>Immobilization techniques</subject><subject>immobilized enzymes</subject><subject>Methods. Procedures. 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Psychology</topic><topic>Immobilization of enzymes and other molecules</topic><topic>Immobilization techniques</topic><topic>immobilized enzymes</topic><topic>Methods. Procedures. Technologies</topic><topic>thermal stability</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Dumitriu, Severian</creatorcontrib><creatorcontrib>Popa, Marcel</creatorcontrib><creatorcontrib>Artenie, Vlad</creatorcontrib><creatorcontrib>Dan, Florin</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</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>Dumitriu, Severian</au><au>Popa, Marcel</au><au>Artenie, Vlad</au><au>Dan, Florin</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Bioactive polymers. 56: Urease immobilization on carboxymethylcellulose</atitle><jtitle>Biotechnology and bioengineering</jtitle><addtitle>Biotechnol. Bioeng</addtitle><date>1989-07</date><risdate>1989</risdate><volume>34</volume><issue>3</issue><spage>283</spage><epage>290</epage><pages>283-290</pages><issn>0006-3592</issn><eissn>1097-0290</eissn><coden>BIBIAU</coden><abstract>This article reports on the reaction of urease immobilization through its covalent bonding on carboxymethylcellulose. The reaction is activated by dicyclohexylcarbodiimide. The coupling reaction is influenced by the enzyme–support and activator–support ratios, as well as by duration. Starting from a rotating, composed experimental program of the second order, the function correlating the activity of the immobilized enzyme with the reaction parameters is established. Immobilized urease exhibits thermal stability higher than that of free enzyme, regarding both pH and the inhibiting action of some metal ions or organic substances. 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| subjects | Biological and medical sciences Biotechnology dicyclohexylcarbodiimide Enzyme engineering Fundamental and applied biological sciences. Psychology Immobilization of enzymes and other molecules Immobilization techniques immobilized enzymes Methods. Procedures. Technologies thermal stability |
| title | Bioactive polymers. 56: Urease immobilization on carboxymethylcellulose |
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