Synthesis of supermacroporous cryogel for bioreactors continuous starch hydrolysis
A bioreactor was built by means of immobilizing alpha‐amylase from Aspergillus oryzae by encapsulation, through cryopolymerization of acrylamide monomers for the continuous starch hydrolysis. The starch hydrolysis was evaluated regarding pH, the concentration of immobilized amylase on cryogel, the c...
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| Veröffentlicht in: | Electrophoresis 2017-11, Vol.38 (22-23), p.2940-2946 |
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| creator | Guilherme, Ederson Paulo Xavier Oliveira, Jocilane Pereira Carvalho, Lorendane Millena Brandi, Igor Viana Santos, Sérgio Henrique Sousa Carvalho, Gleidson Giordano Pinto Cota, Junio Mara Aparecida de Carvalho, Bruna |
| description | A bioreactor was built by means of immobilizing alpha‐amylase from Aspergillus oryzae by encapsulation, through cryopolymerization of acrylamide monomers for the continuous starch hydrolysis. The starch hydrolysis was evaluated regarding pH, the concentration of immobilized amylase on cryogel, the concentration of starch solution and temperature. The maximum value for starch hydrolysis was achieved at pH 5.0, concentration of immobilized enzyme 111.44 mg amylase/gcryogel, concentration of starch solution 45 g/L and temperature of 35°C. The immobilized enzyme showed a conversion ratio ranging from 68.2 to 97.37%, depending on the pH and temperature employed. Thus, our results suggest that the alpha‐amylase from A. oryzae immobilized on cryogel monoliths represents a potential process for industrial production of maltose from starch hydrolysis. |
| doi_str_mv | 10.1002/elps.201700208 |
| format | Article |
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The starch hydrolysis was evaluated regarding pH, the concentration of immobilized amylase on cryogel, the concentration of starch solution and temperature. The maximum value for starch hydrolysis was achieved at pH 5.0, concentration of immobilized enzyme 111.44 mg amylase/gcryogel, concentration of starch solution 45 g/L and temperature of 35°C. The immobilized enzyme showed a conversion ratio ranging from 68.2 to 97.37%, depending on the pH and temperature employed. Thus, our results suggest that the alpha‐amylase from A. oryzae immobilized on cryogel monoliths represents a potential process for industrial production of maltose from starch hydrolysis.</description><identifier>ISSN: 0173-0835</identifier><identifier>EISSN: 1522-2683</identifier><identifier>DOI: 10.1002/elps.201700208</identifier><identifier>PMID: 28777449</identifier><language>eng</language><publisher>Germany: Wiley Subscription Services, Inc</publisher><subject>Acrylamide ; Amylase ; Amylases ; Bioreactors ; Conversion ratio ; Cryogel ; Enzymes ; Hydrolysis ; Maltose ; Monolith</subject><ispartof>Electrophoresis, 2017-11, Vol.38 (22-23), p.2940-2946</ispartof><rights>2017 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim</rights><rights>2017 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.</rights><rights>2017 WILEY-VCH Verlag GmbH & Co. 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The starch hydrolysis was evaluated regarding pH, the concentration of immobilized amylase on cryogel, the concentration of starch solution and temperature. The maximum value for starch hydrolysis was achieved at pH 5.0, concentration of immobilized enzyme 111.44 mg amylase/gcryogel, concentration of starch solution 45 g/L and temperature of 35°C. The immobilized enzyme showed a conversion ratio ranging from 68.2 to 97.37%, depending on the pH and temperature employed. Thus, our results suggest that the alpha‐amylase from A. oryzae immobilized on cryogel monoliths represents a potential process for industrial production of maltose from starch hydrolysis.</description><subject>Acrylamide</subject><subject>Amylase</subject><subject>Amylases</subject><subject>Bioreactors</subject><subject>Conversion ratio</subject><subject>Cryogel</subject><subject>Enzymes</subject><subject>Hydrolysis</subject><subject>Maltose</subject><subject>Monolith</subject><issn>0173-0835</issn><issn>1522-2683</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><recordid>eNqFkEtLxDAUhYMozvjYupSCGzcdkzSvLkXGBwwoPtYlTW-cSqepSYv035syOgs3ri738J3DvQehM4IXBGN6BU0XFhQTGRes9tCccEpTKlS2j-ZRzlKsMj5DRyF8YIxZztghmlElpWQsn6Pnl7Ht1xDqkDibhKEDv9HGu855N4TE-NG9Q5NY55Oydh606Z2Pumv7uh0mJPTam3WyHivvmjEGnaADq5sApz_zGL3dLl9v7tPV493DzfUqNQxzmWYlWK1zI0DZSoPSgkvDpQVCVcmjICzw3ApZyZxzW2rIqwpbo4w0GSMkO0aX29zOu88BQl9s6mCgaXQL8bCC5FQIxTie0Is_6IcbfBuvi5TEnEtJRaQWWyr-H4IHW3S-3mg_FgQXU9vF1Haxazsazn9ih3ID1Q7_rTcCbAt81Q2M_8QVy9XTi4je7BuqyI3K</recordid><startdate>201711</startdate><enddate>201711</enddate><creator>Guilherme, Ederson Paulo Xavier</creator><creator>Oliveira, Jocilane Pereira</creator><creator>Carvalho, Lorendane Millena</creator><creator>Brandi, Igor Viana</creator><creator>Santos, Sérgio Henrique Sousa</creator><creator>Carvalho, Gleidson Giordano Pinto</creator><creator>Cota, Junio</creator><creator>Mara Aparecida de Carvalho, Bruna</creator><general>Wiley Subscription Services, Inc</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7U5</scope><scope>8FD</scope><scope>L7M</scope><scope>7X8</scope></search><sort><creationdate>201711</creationdate><title>Synthesis of supermacroporous cryogel for bioreactors continuous starch hydrolysis</title><author>Guilherme, Ederson Paulo Xavier ; Oliveira, Jocilane Pereira ; Carvalho, Lorendane Millena ; Brandi, Igor Viana ; Santos, Sérgio Henrique Sousa ; Carvalho, Gleidson Giordano Pinto ; Cota, Junio ; Mara Aparecida de Carvalho, Bruna</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4057-3befaa9c6e8fdae8a657c57fe128b5ae86fe59f67d7955fbae9dd0fc8c7c34113</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Acrylamide</topic><topic>Amylase</topic><topic>Amylases</topic><topic>Bioreactors</topic><topic>Conversion ratio</topic><topic>Cryogel</topic><topic>Enzymes</topic><topic>Hydrolysis</topic><topic>Maltose</topic><topic>Monolith</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Guilherme, Ederson Paulo Xavier</creatorcontrib><creatorcontrib>Oliveira, Jocilane Pereira</creatorcontrib><creatorcontrib>Carvalho, Lorendane Millena</creatorcontrib><creatorcontrib>Brandi, Igor Viana</creatorcontrib><creatorcontrib>Santos, Sérgio Henrique Sousa</creatorcontrib><creatorcontrib>Carvalho, Gleidson Giordano Pinto</creatorcontrib><creatorcontrib>Cota, Junio</creatorcontrib><creatorcontrib>Mara Aparecida de Carvalho, Bruna</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Technology Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>MEDLINE - Academic</collection><jtitle>Electrophoresis</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Guilherme, Ederson Paulo Xavier</au><au>Oliveira, Jocilane Pereira</au><au>Carvalho, Lorendane Millena</au><au>Brandi, Igor Viana</au><au>Santos, Sérgio Henrique Sousa</au><au>Carvalho, Gleidson Giordano Pinto</au><au>Cota, Junio</au><au>Mara Aparecida de Carvalho, Bruna</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Synthesis of supermacroporous cryogel for bioreactors continuous starch hydrolysis</atitle><jtitle>Electrophoresis</jtitle><addtitle>Electrophoresis</addtitle><date>2017-11</date><risdate>2017</risdate><volume>38</volume><issue>22-23</issue><spage>2940</spage><epage>2946</epage><pages>2940-2946</pages><issn>0173-0835</issn><eissn>1522-2683</eissn><abstract>A bioreactor was built by means of immobilizing alpha‐amylase from Aspergillus oryzae by encapsulation, through cryopolymerization of acrylamide monomers for the continuous starch hydrolysis. The starch hydrolysis was evaluated regarding pH, the concentration of immobilized amylase on cryogel, the concentration of starch solution and temperature. The maximum value for starch hydrolysis was achieved at pH 5.0, concentration of immobilized enzyme 111.44 mg amylase/gcryogel, concentration of starch solution 45 g/L and temperature of 35°C. The immobilized enzyme showed a conversion ratio ranging from 68.2 to 97.37%, depending on the pH and temperature employed. Thus, our results suggest that the alpha‐amylase from A. oryzae immobilized on cryogel monoliths represents a potential process for industrial production of maltose from starch hydrolysis.</abstract><cop>Germany</cop><pub>Wiley Subscription Services, Inc</pub><pmid>28777449</pmid><doi>10.1002/elps.201700208</doi><tpages>7</tpages></addata></record> |
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| subjects | Acrylamide Amylase Amylases Bioreactors Conversion ratio Cryogel Enzymes Hydrolysis Maltose Monolith |
| title | Synthesis of supermacroporous cryogel for bioreactors continuous starch hydrolysis |
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