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Sucrose hydrolysis by invertase immobilized on Duolite A-568 employing a packed-bed reactor
The conversion of sucrose to a highly concentrated commercial syrup by immobilized invertase by combining the processes of adsorption and cross-linking using Duolite A-568 as the carrier was studied. Central Composite Design (CCD) was used to assess the effect of glutaraldehyde concentration and cro...
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Published in: | Chemical engineering communications 2017-09, Vol.204 (9), p.1007-1019 |
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creator | Cabral, Bruna Vieira Santos, Líbia Diniz Santana Falleiros, Larissa N. S. Carmo, Taciana S. Freitas, Fernanda Ferreira Cardoso, Saulo Luiz Resende, Miriam M. Ribeiro, Eloízio Júlio |
description | The conversion of sucrose to a highly concentrated commercial syrup by immobilized invertase by combining the processes of adsorption and cross-linking using Duolite A-568 as the carrier was studied. Central Composite Design (CCD) was used to assess the effect of glutaraldehyde concentration and cross-linking reaction time on immobilized enzyme activity throughout the hydrolysis of sucrose in a batch reactor. Cross-linking optimization allowed us to find the optimum conditions for activity with a glutaraldehyde concentration of 0.6 g · L
−1
and a cross-linking time of 6 h. The temperature and pH that maximized the activity of the immobilized biocatalyst in the cross-linking process were 50°C and 4.0, respectively. Cross-linking allows the biocatalyst to be active at higher temperatures and lower pH. High-sucrose conversions to invert sugar using a continuous fixed-bed reactor were obtained. The immobilized biocatalyst also demonstrated greater thermal stability at low temperatures. |
doi_str_mv | 10.1080/00986445.2017.1336089 |
format | article |
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−1
and a cross-linking time of 6 h. The temperature and pH that maximized the activity of the immobilized biocatalyst in the cross-linking process were 50°C and 4.0, respectively. Cross-linking allows the biocatalyst to be active at higher temperatures and lower pH. High-sucrose conversions to invert sugar using a continuous fixed-bed reactor were obtained. The immobilized biocatalyst also demonstrated greater thermal stability at low temperatures.</description><identifier>ISSN: 0098-6445</identifier><identifier>EISSN: 1563-5201</identifier><identifier>DOI: 10.1080/00986445.2017.1336089</identifier><language>eng</language><publisher>Philadelphia: Taylor & Francis</publisher><subject>Adsorption ; Biocatalysts ; Crosslinking ; Enzyme activity ; Glutaraldehyde ; Hydrolysis ; immobilization ; Invertase ; Reaction time ; resin Duolite A-568 ; Sucrose ; Syrup ; Thermal stability</subject><ispartof>Chemical engineering communications, 2017-09, Vol.204 (9), p.1007-1019</ispartof><rights>2017 Taylor & Francis 2017</rights><rights>2017 Taylor & Francis</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c375t-d11b5806e9798f1161ff88c37ade34362bd0047b1075568a2cc1e4baf376799d3</citedby><cites>FETCH-LOGICAL-c375t-d11b5806e9798f1161ff88c37ade34362bd0047b1075568a2cc1e4baf376799d3</cites><orcidid>0000-0002-2308-1523</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27923,27924</link.rule.ids></links><search><creatorcontrib>Cabral, Bruna Vieira</creatorcontrib><creatorcontrib>Santos, Líbia Diniz</creatorcontrib><creatorcontrib>Santana Falleiros, Larissa N. S.</creatorcontrib><creatorcontrib>Carmo, Taciana S.</creatorcontrib><creatorcontrib>Freitas, Fernanda Ferreira</creatorcontrib><creatorcontrib>Cardoso, Saulo Luiz</creatorcontrib><creatorcontrib>Resende, Miriam M.</creatorcontrib><creatorcontrib>Ribeiro, Eloízio Júlio</creatorcontrib><title>Sucrose hydrolysis by invertase immobilized on Duolite A-568 employing a packed-bed reactor</title><title>Chemical engineering communications</title><description>The conversion of sucrose to a highly concentrated commercial syrup by immobilized invertase by combining the processes of adsorption and cross-linking using Duolite A-568 as the carrier was studied. Central Composite Design (CCD) was used to assess the effect of glutaraldehyde concentration and cross-linking reaction time on immobilized enzyme activity throughout the hydrolysis of sucrose in a batch reactor. Cross-linking optimization allowed us to find the optimum conditions for activity with a glutaraldehyde concentration of 0.6 g · L
−1
and a cross-linking time of 6 h. The temperature and pH that maximized the activity of the immobilized biocatalyst in the cross-linking process were 50°C and 4.0, respectively. Cross-linking allows the biocatalyst to be active at higher temperatures and lower pH. High-sucrose conversions to invert sugar using a continuous fixed-bed reactor were obtained. The immobilized biocatalyst also demonstrated greater thermal stability at low temperatures.</description><subject>Adsorption</subject><subject>Biocatalysts</subject><subject>Crosslinking</subject><subject>Enzyme activity</subject><subject>Glutaraldehyde</subject><subject>Hydrolysis</subject><subject>immobilization</subject><subject>Invertase</subject><subject>Reaction time</subject><subject>resin Duolite A-568</subject><subject>Sucrose</subject><subject>Syrup</subject><subject>Thermal stability</subject><issn>0098-6445</issn><issn>1563-5201</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><recordid>eNp9kE9LxDAQxYMouK5-BCHguWtm06bpzWX9Cwse1JOHkDaJZm2bmrRK_fSm7Hr1NPDm994wD6FzIAsgnFwSUnCWptliSSBfAKWM8OIAzSBjNMmieIhmE5NM0DE6CWFLSMQAZuj1aai8Cxq_j8q7egw24HLEtv3SvpdRt03jSlvbH62wa_H14Grba7xKMsaxbrrajbZ9wxJ3svrQKikj57WseudP0ZGRddBn-zlHL7c3z-v7ZPN497BebZKK5lmfKIAy44TpIi-4AWBgDOdxJ5WmKWXLUhGS5iWQPItH5bKqQKelNDRneVEoOkcXu9zOu89Bh15s3eDbeFJAEROApoxHKttR07_BayM6bxvpRwFETD2Kvx7F1KPY9xh9VzufbY3zjfx2vlail2PtvPGyrWwQ9P-IXzg2eOM</recordid><startdate>20170902</startdate><enddate>20170902</enddate><creator>Cabral, Bruna Vieira</creator><creator>Santos, Líbia Diniz</creator><creator>Santana Falleiros, Larissa N. S.</creator><creator>Carmo, Taciana S.</creator><creator>Freitas, Fernanda Ferreira</creator><creator>Cardoso, Saulo Luiz</creator><creator>Resende, Miriam M.</creator><creator>Ribeiro, Eloízio Júlio</creator><general>Taylor & Francis</general><general>Taylor & Francis Ltd</general><scope>AAYXX</scope><scope>CITATION</scope><scope>7U5</scope><scope>8FD</scope><scope>L7M</scope><orcidid>https://orcid.org/0000-0002-2308-1523</orcidid></search><sort><creationdate>20170902</creationdate><title>Sucrose hydrolysis by invertase immobilized on Duolite A-568 employing a packed-bed reactor</title><author>Cabral, Bruna Vieira ; Santos, Líbia Diniz ; Santana Falleiros, Larissa N. 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S.</creatorcontrib><creatorcontrib>Carmo, Taciana S.</creatorcontrib><creatorcontrib>Freitas, Fernanda Ferreira</creatorcontrib><creatorcontrib>Cardoso, Saulo Luiz</creatorcontrib><creatorcontrib>Resende, Miriam M.</creatorcontrib><creatorcontrib>Ribeiro, Eloízio Júlio</creatorcontrib><collection>CrossRef</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Technology Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><jtitle>Chemical engineering communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cabral, Bruna Vieira</au><au>Santos, Líbia Diniz</au><au>Santana Falleiros, Larissa N. S.</au><au>Carmo, Taciana S.</au><au>Freitas, Fernanda Ferreira</au><au>Cardoso, Saulo Luiz</au><au>Resende, Miriam M.</au><au>Ribeiro, Eloízio Júlio</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Sucrose hydrolysis by invertase immobilized on Duolite A-568 employing a packed-bed reactor</atitle><jtitle>Chemical engineering communications</jtitle><date>2017-09-02</date><risdate>2017</risdate><volume>204</volume><issue>9</issue><spage>1007</spage><epage>1019</epage><pages>1007-1019</pages><issn>0098-6445</issn><eissn>1563-5201</eissn><abstract>The conversion of sucrose to a highly concentrated commercial syrup by immobilized invertase by combining the processes of adsorption and cross-linking using Duolite A-568 as the carrier was studied. Central Composite Design (CCD) was used to assess the effect of glutaraldehyde concentration and cross-linking reaction time on immobilized enzyme activity throughout the hydrolysis of sucrose in a batch reactor. Cross-linking optimization allowed us to find the optimum conditions for activity with a glutaraldehyde concentration of 0.6 g · L
−1
and a cross-linking time of 6 h. The temperature and pH that maximized the activity of the immobilized biocatalyst in the cross-linking process were 50°C and 4.0, respectively. Cross-linking allows the biocatalyst to be active at higher temperatures and lower pH. High-sucrose conversions to invert sugar using a continuous fixed-bed reactor were obtained. The immobilized biocatalyst also demonstrated greater thermal stability at low temperatures.</abstract><cop>Philadelphia</cop><pub>Taylor & Francis</pub><doi>10.1080/00986445.2017.1336089</doi><tpages>13</tpages><orcidid>https://orcid.org/0000-0002-2308-1523</orcidid></addata></record> |
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subjects | Adsorption Biocatalysts Crosslinking Enzyme activity Glutaraldehyde Hydrolysis immobilization Invertase Reaction time resin Duolite A-568 Sucrose Syrup Thermal stability |
title | Sucrose hydrolysis by invertase immobilized on Duolite A-568 employing a packed-bed reactor |
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