Functional stabilization of cellulase by covalent modification with chitosan
Chitosan was linked to cellulase (EC 3.2.1.4) from Trichoderma viride by covalent conjugation to periodate‐activated carbohydrate moieties of the enzyme. The modified enzyme contained about 1.5 mol of polymer per mol of protein. The specific activity of the conjugate prepared was 39.8% of the native...
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| Veröffentlicht in: | Journal of chemical technology and biotechnology (1986) 2001-05, Vol.76 (5), p.489-493 |
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| container_end_page | 493 |
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| container_title | Journal of chemical technology and biotechnology (1986) |
| container_volume | 76 |
| creator | Darias, Rodolfo Villalonga, Reynaldo |
| description | Chitosan was linked to cellulase (EC 3.2.1.4) from Trichoderma viride by covalent conjugation to periodate‐activated carbohydrate moieties of the enzyme. The modified enzyme contained about 1.5 mol of polymer per mol of protein. The specific activity of the conjugate prepared was 39.8% of the native cellulase. The optimum pH and temperature for cellulase remained unaltered after modification. The thermostability was increased by 8.9 °C for the cellulase–chitosan complex. Thermal inactivation at different temperatures ranging from 65 °C to 80 °C was markedly increased for the polymer‐modified enzyme. The stability within the pH range 1.0–3.2 was also improved for the modified enzyme.
© 2001 Society of Chemical Industry |
| doi_str_mv | 10.1002/jctb.386 |
| format | Article |
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© 2001 Society of Chemical Industry</description><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>cellulase</subject><subject>Chemical synthesis for preparing modified enzymes, enzyme fragments and enzyme analogs</subject><subject>chitosan</subject><subject>Enzyme engineering</subject><subject>enzyme stability</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>glycoenzyme</subject><subject>Methods. Procedures. Technologies</subject><subject>modified enzyme</subject><subject>Production of selected enzymes</subject><issn>0268-2575</issn><issn>1097-4660</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><recordid>eNp10NFKwzAUBuAgCs4p-AgFQbzpTJMlaS51uOmYijBRvAmnacIys3Y2nXM-vR0du_PqcA4fP4cfofME9xKMyfVc11mPpvwAdRIsRdznHB-iDiY8jQkT7BidhDDHGPOU8A6aDFeFrl1ZgI9CDZnz7he2e1TaSBvvVx6CibJNpMtv8Kaoo0WZO-t0q9aunkV65uoyQHGKjiz4YM52s4teh3fTwX08eR49DG4msaZS8FgTQpmhOkvB8Fzj5sooS_sMk0RayRKbg6QJMJ6B0FaK3GAjNU4zS3KwCe2iyzZ3WZVfKxNqtXBh-ywUplwFRbigkvRFA69aqKsyhMpYtazcAqqNSrDa1qW2dammroZe7DIhaPC2gkK7sPdSSIlpo-JWrZ03m3_T1HgwvW1Td96F2vzsPVSfqvlRMPX2NFKDl4-xeKTvakz_AKkgiWY</recordid><startdate>200105</startdate><enddate>200105</enddate><creator>Darias, Rodolfo</creator><creator>Villalonga, Reynaldo</creator><general>John Wiley & Sons, Ltd</general><general>Wiley</general><scope>BSCLL</scope><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>8FD</scope><scope>F28</scope><scope>FR3</scope></search><sort><creationdate>200105</creationdate><title>Functional stabilization of cellulase by covalent modification with chitosan</title><author>Darias, Rodolfo ; Villalonga, Reynaldo</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3976-c2235e3cb8ae6dc0c395358450219f951fda931a56ba7cf97de0e9c08bf2daf13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>cellulase</topic><topic>Chemical synthesis for preparing modified enzymes, enzyme fragments and enzyme analogs</topic><topic>chitosan</topic><topic>Enzyme engineering</topic><topic>enzyme stability</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>glycoenzyme</topic><topic>Methods. Procedures. Technologies</topic><topic>modified enzyme</topic><topic>Production of selected enzymes</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Darias, Rodolfo</creatorcontrib><creatorcontrib>Villalonga, Reynaldo</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>ANTE: Abstracts in New Technology & Engineering</collection><collection>Engineering Research Database</collection><jtitle>Journal of chemical technology and biotechnology (1986)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Darias, Rodolfo</au><au>Villalonga, Reynaldo</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Functional stabilization of cellulase by covalent modification with chitosan</atitle><jtitle>Journal of chemical technology and biotechnology (1986)</jtitle><addtitle>J. Chem. Technol. Biotechnol</addtitle><date>2001-05</date><risdate>2001</risdate><volume>76</volume><issue>5</issue><spage>489</spage><epage>493</epage><pages>489-493</pages><issn>0268-2575</issn><eissn>1097-4660</eissn><coden>JCTBDC</coden><abstract>Chitosan was linked to cellulase (EC 3.2.1.4) from Trichoderma viride by covalent conjugation to periodate‐activated carbohydrate moieties of the enzyme. The modified enzyme contained about 1.5 mol of polymer per mol of protein. The specific activity of the conjugate prepared was 39.8% of the native cellulase. The optimum pH and temperature for cellulase remained unaltered after modification. The thermostability was increased by 8.9 °C for the cellulase–chitosan complex. Thermal inactivation at different temperatures ranging from 65 °C to 80 °C was markedly increased for the polymer‐modified enzyme. The stability within the pH range 1.0–3.2 was also improved for the modified enzyme.
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| ispartof | Journal of chemical technology and biotechnology (1986), 2001-05, Vol.76 (5), p.489-493 |
| issn | 0268-2575 1097-4660 |
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| subjects | Biological and medical sciences Biotechnology cellulase Chemical synthesis for preparing modified enzymes, enzyme fragments and enzyme analogs chitosan Enzyme engineering enzyme stability Fundamental and applied biological sciences. Psychology glycoenzyme Methods. Procedures. Technologies modified enzyme Production of selected enzymes |
| title | Functional stabilization of cellulase by covalent modification with chitosan |
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