Lipase immobilization on high water adsorbing capacity bagasse: applications in bio-based plasticizer synthesis
This study investigates the structure and water adsorbing capacity of bagasse and of sodium hydroxide pretreated bagasse. The structures of bagasse and bagasse-NaOH were compared by SEM and XRD. Candida antarctica lipase B was then immobilized on bagasse, bagasse-NaOH and DPA@bagasse-NaOH. The expre...
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| Veröffentlicht in: | Molecular biology reports 2018-12, Vol.45 (6), p.2095-2102 |
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| description | This study investigates the structure and water adsorbing capacity of bagasse and of sodium hydroxide pretreated bagasse. The structures of bagasse and bagasse-NaOH were compared by SEM and XRD.
Candida antarctica
lipase B was then immobilized on bagasse, bagasse-NaOH and DPA@bagasse-NaOH. The expressed activity and immobilization yield of lipase immobilized on bagasse-NaOH (1.0%) was 36% and 45% higher than that on bagasse. When dopamine (DPA) was used as cationic polymer monomer via self-polymerization for mediating immobilization, the protein loading amounts and activity of lipase immobilized on DPA@bagasse-NaOH were higher than that of bagasse-NaOH. When the DPA concentration was 100 mg/ml, the immobilized lipase expressed activity reached its highest value (800 U/g), where the immobilization yield achieved 96.8%, which was 3.93-fold of lipase immobilized on native bagasse (24.6%). Then the immobilized lipases were used to synthesize a bio-based plasticizer. Lipase immobilized on DPA@bagasse-NaOH exhibited a significantly improved operational stability. Even after 12 batches, a high ester yield (84.2%) was maintained. Additionally, poly (vinyl chloride) PVC blends plasticized with methyl oleate as a secondary plasticizer were investigated. It was discovered that methyl oleate can be used as an effective bio-based plasticizer for PVC. These results indicate that bagasse with high water adsorbing capacity and self-polymerized DPA layer could create a favorable microenvironment for bio-based plasticizer synthesis in esterification reactions. |
| doi_str_mv | 10.1007/s11033-018-4366-6 |
| format | Article |
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Candida antarctica
lipase B was then immobilized on bagasse, bagasse-NaOH and DPA@bagasse-NaOH. The expressed activity and immobilization yield of lipase immobilized on bagasse-NaOH (1.0%) was 36% and 45% higher than that on bagasse. When dopamine (DPA) was used as cationic polymer monomer via self-polymerization for mediating immobilization, the protein loading amounts and activity of lipase immobilized on DPA@bagasse-NaOH were higher than that of bagasse-NaOH. When the DPA concentration was 100 mg/ml, the immobilized lipase expressed activity reached its highest value (800 U/g), where the immobilization yield achieved 96.8%, which was 3.93-fold of lipase immobilized on native bagasse (24.6%). Then the immobilized lipases were used to synthesize a bio-based plasticizer. Lipase immobilized on DPA@bagasse-NaOH exhibited a significantly improved operational stability. Even after 12 batches, a high ester yield (84.2%) was maintained. Additionally, poly (vinyl chloride) PVC blends plasticized with methyl oleate as a secondary plasticizer were investigated. It was discovered that methyl oleate can be used as an effective bio-based plasticizer for PVC. These results indicate that bagasse with high water adsorbing capacity and self-polymerized DPA layer could create a favorable microenvironment for bio-based plasticizer synthesis in esterification reactions.</description><identifier>ISSN: 0301-4851</identifier><identifier>EISSN: 1573-4978</identifier><identifier>DOI: 10.1007/s11033-018-4366-6</identifier><identifier>PMID: 30209742</identifier><language>eng</language><publisher>Dordrecht: Springer Netherlands</publisher><subject>Animal Anatomy ; Animal Biochemistry ; Bagasse ; Biocatalysis ; Biomedical and Life Sciences ; Cellulose - chemistry ; Dopamine ; Enzymes, Immobilized ; Esterification ; Esters ; Fungal Proteins - chemistry ; Fungal Proteins - metabolism ; Histology ; Hydrogen-Ion Concentration ; Immobilization ; Life Sciences ; Lipase ; Lipase - chemistry ; Lipase - metabolism ; Morphology ; Original Article ; Plasticizers - chemistry ; Polymerization ; Polyvinyl chloride ; Sodium ; Sodium hydroxide ; Sodium Hydroxide - chemistry ; Vinyl chloride ; Water</subject><ispartof>Molecular biology reports, 2018-12, Vol.45 (6), p.2095-2102</ispartof><rights>Springer Nature B.V. 2018</rights><rights>Molecular Biology Reports is a copyright of Springer, (2018). All Rights Reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c372t-be1b1260395ac6acd97b79f10d069b0dedf573f5092451d5c151dfa057614f363</citedby><cites>FETCH-LOGICAL-c372t-be1b1260395ac6acd97b79f10d069b0dedf573f5092451d5c151dfa057614f363</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s11033-018-4366-6$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s11033-018-4366-6$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/30209742$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Cui, Caixia</creatorcontrib><creatorcontrib>Cai, Di</creatorcontrib><title>Lipase immobilization on high water adsorbing capacity bagasse: applications in bio-based plasticizer synthesis</title><title>Molecular biology reports</title><addtitle>Mol Biol Rep</addtitle><addtitle>Mol Biol Rep</addtitle><description>This study investigates the structure and water adsorbing capacity of bagasse and of sodium hydroxide pretreated bagasse. The structures of bagasse and bagasse-NaOH were compared by SEM and XRD.
Candida antarctica
lipase B was then immobilized on bagasse, bagasse-NaOH and DPA@bagasse-NaOH. The expressed activity and immobilization yield of lipase immobilized on bagasse-NaOH (1.0%) was 36% and 45% higher than that on bagasse. When dopamine (DPA) was used as cationic polymer monomer via self-polymerization for mediating immobilization, the protein loading amounts and activity of lipase immobilized on DPA@bagasse-NaOH were higher than that of bagasse-NaOH. When the DPA concentration was 100 mg/ml, the immobilized lipase expressed activity reached its highest value (800 U/g), where the immobilization yield achieved 96.8%, which was 3.93-fold of lipase immobilized on native bagasse (24.6%). Then the immobilized lipases were used to synthesize a bio-based plasticizer. Lipase immobilized on DPA@bagasse-NaOH exhibited a significantly improved operational stability. Even after 12 batches, a high ester yield (84.2%) was maintained. Additionally, poly (vinyl chloride) PVC blends plasticized with methyl oleate as a secondary plasticizer were investigated. It was discovered that methyl oleate can be used as an effective bio-based plasticizer for PVC. These results indicate that bagasse with high water adsorbing capacity and self-polymerized DPA layer could create a favorable microenvironment for bio-based plasticizer synthesis in esterification reactions.</description><subject>Animal Anatomy</subject><subject>Animal Biochemistry</subject><subject>Bagasse</subject><subject>Biocatalysis</subject><subject>Biomedical and Life Sciences</subject><subject>Cellulose - chemistry</subject><subject>Dopamine</subject><subject>Enzymes, Immobilized</subject><subject>Esterification</subject><subject>Esters</subject><subject>Fungal Proteins - chemistry</subject><subject>Fungal Proteins - metabolism</subject><subject>Histology</subject><subject>Hydrogen-Ion Concentration</subject><subject>Immobilization</subject><subject>Life Sciences</subject><subject>Lipase</subject><subject>Lipase - chemistry</subject><subject>Lipase - metabolism</subject><subject>Morphology</subject><subject>Original Article</subject><subject>Plasticizers - chemistry</subject><subject>Polymerization</subject><subject>Polyvinyl chloride</subject><subject>Sodium</subject><subject>Sodium hydroxide</subject><subject>Sodium Hydroxide - chemistry</subject><subject>Vinyl chloride</subject><subject>Water</subject><issn>0301-4851</issn><issn>1573-4978</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp1kU2LFDEQhoMo7rj6A7xIwIuXaKXz1e1NltVdGPCi55Ck0zNZujttqgeZ_fVmdlYFQQjJIU89qdRLyGsO7zmA-YCcgxAMeMuk0JrpJ2TDlRFMdqZ9SjYggDPZKn5BXiDeAYDkRj0nFwIa6IxsNiRv0-Iw0jRN2acx3bs15ZnWtU-7Pf3p1lio6zEXn-YdDW5xIa1H6t3OIcaP1C3LmMJDFdI0U58y89XY02V0uKaQ7qsBj_O6j5jwJXk2uBHjq8fzknz_fP3t6oZtv365vfq0ZUGYZmU-cs8bDaJTLmgX-s540w0cetCdhz72Q_3noKBrpOK9CrzugwNlNJeD0OKSvDt7l5J_HCKudkoY4ji6OeYD2qZOThshpKzo23_Qu3woc-3ugRKqbU1bKX6mQsmIJQ52KWly5Wg52FMa9pyGrWnYUxr21MSbR_PBT7H_U_F7_BVozgDWq3kXy9-n_2_9BTzKlbg</recordid><startdate>20181201</startdate><enddate>20181201</enddate><creator>Cui, Caixia</creator><creator>Cai, Di</creator><general>Springer Netherlands</general><general>Springer Nature B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7TK</scope><scope>7TM</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20181201</creationdate><title>Lipase immobilization on high water adsorbing capacity bagasse: applications in bio-based plasticizer synthesis</title><author>Cui, Caixia ; Cai, Di</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c372t-be1b1260395ac6acd97b79f10d069b0dedf573f5092451d5c151dfa057614f363</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Animal Anatomy</topic><topic>Animal Biochemistry</topic><topic>Bagasse</topic><topic>Biocatalysis</topic><topic>Biomedical and Life Sciences</topic><topic>Cellulose - chemistry</topic><topic>Dopamine</topic><topic>Enzymes, Immobilized</topic><topic>Esterification</topic><topic>Esters</topic><topic>Fungal Proteins - chemistry</topic><topic>Fungal Proteins - metabolism</topic><topic>Histology</topic><topic>Hydrogen-Ion Concentration</topic><topic>Immobilization</topic><topic>Life Sciences</topic><topic>Lipase</topic><topic>Lipase - chemistry</topic><topic>Lipase - metabolism</topic><topic>Morphology</topic><topic>Original Article</topic><topic>Plasticizers - chemistry</topic><topic>Polymerization</topic><topic>Polyvinyl chloride</topic><topic>Sodium</topic><topic>Sodium hydroxide</topic><topic>Sodium Hydroxide - chemistry</topic><topic>Vinyl chloride</topic><topic>Water</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cui, Caixia</creatorcontrib><creatorcontrib>Cai, Di</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular biology reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cui, Caixia</au><au>Cai, Di</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Lipase immobilization on high water adsorbing capacity bagasse: applications in bio-based plasticizer synthesis</atitle><jtitle>Molecular biology reports</jtitle><stitle>Mol Biol Rep</stitle><addtitle>Mol Biol Rep</addtitle><date>2018-12-01</date><risdate>2018</risdate><volume>45</volume><issue>6</issue><spage>2095</spage><epage>2102</epage><pages>2095-2102</pages><issn>0301-4851</issn><eissn>1573-4978</eissn><abstract>This study investigates the structure and water adsorbing capacity of bagasse and of sodium hydroxide pretreated bagasse. The structures of bagasse and bagasse-NaOH were compared by SEM and XRD.
Candida antarctica
lipase B was then immobilized on bagasse, bagasse-NaOH and DPA@bagasse-NaOH. The expressed activity and immobilization yield of lipase immobilized on bagasse-NaOH (1.0%) was 36% and 45% higher than that on bagasse. When dopamine (DPA) was used as cationic polymer monomer via self-polymerization for mediating immobilization, the protein loading amounts and activity of lipase immobilized on DPA@bagasse-NaOH were higher than that of bagasse-NaOH. When the DPA concentration was 100 mg/ml, the immobilized lipase expressed activity reached its highest value (800 U/g), where the immobilization yield achieved 96.8%, which was 3.93-fold of lipase immobilized on native bagasse (24.6%). Then the immobilized lipases were used to synthesize a bio-based plasticizer. Lipase immobilized on DPA@bagasse-NaOH exhibited a significantly improved operational stability. Even after 12 batches, a high ester yield (84.2%) was maintained. Additionally, poly (vinyl chloride) PVC blends plasticized with methyl oleate as a secondary plasticizer were investigated. It was discovered that methyl oleate can be used as an effective bio-based plasticizer for PVC. These results indicate that bagasse with high water adsorbing capacity and self-polymerized DPA layer could create a favorable microenvironment for bio-based plasticizer synthesis in esterification reactions.</abstract><cop>Dordrecht</cop><pub>Springer Netherlands</pub><pmid>30209742</pmid><doi>10.1007/s11033-018-4366-6</doi><tpages>8</tpages></addata></record> |
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| subjects | Animal Anatomy Animal Biochemistry Bagasse Biocatalysis Biomedical and Life Sciences Cellulose - chemistry Dopamine Enzymes, Immobilized Esterification Esters Fungal Proteins - chemistry Fungal Proteins - metabolism Histology Hydrogen-Ion Concentration Immobilization Life Sciences Lipase Lipase - chemistry Lipase - metabolism Morphology Original Article Plasticizers - chemistry Polymerization Polyvinyl chloride Sodium Sodium hydroxide Sodium Hydroxide - chemistry Vinyl chloride Water |
| title | Lipase immobilization on high water adsorbing capacity bagasse: applications in bio-based plasticizer synthesis |
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