On the possibilities of immobilization and utilization of some cellulase enzymes
Cellulase enzymes produced by the microorganisms Aspergillus niger and Trichoderma viride have been immobilized on Ponilex type ion exchangers, both by ionic and by covalent bonding. Immobilization efficiency has been determined for enzyme preparations obtained, by their activity, as well as by that...
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Veröffentlicht in: | Journal of applied polymer science 1990-05, Vol.39 (9), p.1837-1846 |
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container_title | Journal of applied polymer science |
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creator | Simionescu, C.I. (Polytechnic Institute of Jassy, Jassy, Romania) Popa, V.I Popa, M Maxim, S |
description | Cellulase enzymes produced by the microorganisms Aspergillus niger and Trichoderma viride have been immobilized on Ponilex type ion exchangers, both by ionic and by covalent bonding. Immobilization efficiency has been determined for enzyme preparations obtained, by their activity, as well as by that of the resulted effluent, on using as substrate carboxymethyl cellulose, cellobiose, and filter paper. The catalytic activity of the immobilized products has been tested against solutions of carboxymethyl cellulose and a series of hemicellulose containing alkaline extracts resulted from the alkaline pretreatments of some vegetal materials. The presence of polyphenol compounds in the latter ones determines a series of peculiarities in the behavior of the enzyme preparations, such as the transformation of the hydrolysis products and reduction of the catalytic activity of the enzyme, after a certain period of reaction |
doi_str_mv | 10.1002/app.1990.070390902 |
format | Article |
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(Polytechnic Institute of Jassy, Jassy, Romania) ; Popa, V.I ; Popa, M ; Maxim, S</creator><creatorcontrib>Simionescu, C.I. (Polytechnic Institute of Jassy, Jassy, Romania) ; Popa, V.I ; Popa, M ; Maxim, S</creatorcontrib><description>Cellulase enzymes produced by the microorganisms Aspergillus niger and Trichoderma viride have been immobilized on Ponilex type ion exchangers, both by ionic and by covalent bonding. Immobilization efficiency has been determined for enzyme preparations obtained, by their activity, as well as by that of the resulted effluent, on using as substrate carboxymethyl cellulose, cellobiose, and filter paper. The catalytic activity of the immobilized products has been tested against solutions of carboxymethyl cellulose and a series of hemicellulose containing alkaline extracts resulted from the alkaline pretreatments of some vegetal materials. The presence of polyphenol compounds in the latter ones determines a series of peculiarities in the behavior of the enzyme preparations, such as the transformation of the hydrolysis products and reduction of the catalytic activity of the enzyme, after a certain period of reaction</description><identifier>ISSN: 0021-8995</identifier><identifier>EISSN: 1097-4628</identifier><identifier>DOI: 10.1002/app.1990.070390902</identifier><identifier>CODEN: JAPNAB</identifier><language>eng</language><publisher>New York: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>ACTIVIDAD ENZIMATICA ; ACTIVITE ENZYMATIQUE ; Applied sciences ; ASPERGILLUS NIGER ; CELLOBIOSE ; CELLULOSE ; CELOBIOSA ; CELULOSA ; Exact sciences and technology ; Exchange resins and membranes ; Forms of application and semi-finished materials ; HIDROLISIS ; HYDROLYSE ; IMMOBILISATION ; INMOVILIZACION ; Polymer industry, paints, wood ; Technology of polymers ; TRICHODERMA</subject><ispartof>Journal of applied polymer science, 1990-05, Vol.39 (9), p.1837-1846</ispartof><rights>Copyright © 1990 John Wiley & Sons, Inc.</rights><rights>1990 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3842-2734bb1699d437b19e445952cbec4d9846d12b5a2fdf6e4c40e837dbba98c62d3</citedby><cites>FETCH-LOGICAL-c3842-2734bb1699d437b19e445952cbec4d9846d12b5a2fdf6e4c40e837dbba98c62d3</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%2Fapp.1990.070390902$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fapp.1990.070390902$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>315,781,785,1418,27929,27930,45579,45580</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=6804714$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Simionescu, C.I. (Polytechnic Institute of Jassy, Jassy, Romania)</creatorcontrib><creatorcontrib>Popa, V.I</creatorcontrib><creatorcontrib>Popa, M</creatorcontrib><creatorcontrib>Maxim, S</creatorcontrib><title>On the possibilities of immobilization and utilization of some cellulase enzymes</title><title>Journal of applied polymer science</title><addtitle>J. Appl. Polym. Sci</addtitle><description>Cellulase enzymes produced by the microorganisms Aspergillus niger and Trichoderma viride have been immobilized on Ponilex type ion exchangers, both by ionic and by covalent bonding. Immobilization efficiency has been determined for enzyme preparations obtained, by their activity, as well as by that of the resulted effluent, on using as substrate carboxymethyl cellulose, cellobiose, and filter paper. The catalytic activity of the immobilized products has been tested against solutions of carboxymethyl cellulose and a series of hemicellulose containing alkaline extracts resulted from the alkaline pretreatments of some vegetal materials. The presence of polyphenol compounds in the latter ones determines a series of peculiarities in the behavior of the enzyme preparations, such as the transformation of the hydrolysis products and reduction of the catalytic activity of the enzyme, after a certain period of reaction</description><subject>ACTIVIDAD ENZIMATICA</subject><subject>ACTIVITE ENZYMATIQUE</subject><subject>Applied sciences</subject><subject>ASPERGILLUS NIGER</subject><subject>CELLOBIOSE</subject><subject>CELLULOSE</subject><subject>CELOBIOSA</subject><subject>CELULOSA</subject><subject>Exact sciences and technology</subject><subject>Exchange resins and membranes</subject><subject>Forms of application and semi-finished materials</subject><subject>HIDROLISIS</subject><subject>HYDROLYSE</subject><subject>IMMOBILISATION</subject><subject>INMOVILIZACION</subject><subject>Polymer industry, paints, wood</subject><subject>Technology of polymers</subject><subject>TRICHODERMA</subject><issn>0021-8995</issn><issn>1097-4628</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><recordid>eNqNkMtOwzAQRS0EEqXwA115wTZl_EgcS2wqHi2igqJSsbQcxwFDXopTQfv1pAoqLFmNRjrnzugiNCIwJgD0Qtf1mEgJYxDAJEigB2hAQIqARzQ-RIMOIkEsZXiMTrx_ByAkhGiAFo8lbt8srivvXeJy1zrrcZVhVxTVbt_q1lUl1mWK1-3v3hG-Kiw2Ns_XufYW23K7Kaw_RUeZzr09-5lDtLq9eb6aBfPH6d3VZB4YFnMaUMF4kpBIypQzkRBpOQ9lSE1iDU9lzKOU0CTUNEuzyHLDwcZMpEmiZWwimrIhon2uabrXG5upunGFbjaKgNp1orpO1K4Tte-kk857qdbe6DxrdGmc35tRDFwQ3mGXPfbpcrv5R7CaLBZ_rwS97nxrv_a6bj5UJJgI1cvDVDGYieXy6V5dd_yo5zNdKf3adB-tlpJQDjRk38dsi-o</recordid><startdate>19900505</startdate><enddate>19900505</enddate><creator>Simionescu, C.I. 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(Polytechnic Institute of Jassy, Jassy, Romania)</creatorcontrib><creatorcontrib>Popa, V.I</creatorcontrib><creatorcontrib>Popa, M</creatorcontrib><creatorcontrib>Maxim, S</creatorcontrib><collection>AGRIS</collection><collection>Istex</collection><collection>Pascal-Francis</collection><collection>CrossRef</collection><jtitle>Journal of applied polymer science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Simionescu, C.I. (Polytechnic Institute of Jassy, Jassy, Romania)</au><au>Popa, V.I</au><au>Popa, M</au><au>Maxim, S</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>On the possibilities of immobilization and utilization of some cellulase enzymes</atitle><jtitle>Journal of applied polymer science</jtitle><addtitle>J. Appl. Polym. Sci</addtitle><date>1990-05-05</date><risdate>1990</risdate><volume>39</volume><issue>9</issue><spage>1837</spage><epage>1846</epage><pages>1837-1846</pages><issn>0021-8995</issn><eissn>1097-4628</eissn><coden>JAPNAB</coden><abstract>Cellulase enzymes produced by the microorganisms Aspergillus niger and Trichoderma viride have been immobilized on Ponilex type ion exchangers, both by ionic and by covalent bonding. Immobilization efficiency has been determined for enzyme preparations obtained, by their activity, as well as by that of the resulted effluent, on using as substrate carboxymethyl cellulose, cellobiose, and filter paper. The catalytic activity of the immobilized products has been tested against solutions of carboxymethyl cellulose and a series of hemicellulose containing alkaline extracts resulted from the alkaline pretreatments of some vegetal materials. The presence of polyphenol compounds in the latter ones determines a series of peculiarities in the behavior of the enzyme preparations, such as the transformation of the hydrolysis products and reduction of the catalytic activity of the enzyme, after a certain period of reaction</abstract><cop>New York</cop><pub>Wiley Subscription Services, Inc., A Wiley Company</pub><doi>10.1002/app.1990.070390902</doi><tpages>10</tpages></addata></record> |
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subjects | ACTIVIDAD ENZIMATICA ACTIVITE ENZYMATIQUE Applied sciences ASPERGILLUS NIGER CELLOBIOSE CELLULOSE CELOBIOSA CELULOSA Exact sciences and technology Exchange resins and membranes Forms of application and semi-finished materials HIDROLISIS HYDROLYSE IMMOBILISATION INMOVILIZACION Polymer industry, paints, wood Technology of polymers TRICHODERMA |
title | On the possibilities of immobilization and utilization of some cellulase enzymes |
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