Magnetic Cross-Linked Enzyme Aggregates of Aspergillus oryzae ST11 Lipase Using Polyacrylonitrile Coated Magnetic Nanoparticles for Biodiesel Production
The biodiesel production by enzymatic catalysis is the environmentally friendly production process. In this work, the polyacrylonitrile coated magnetic nanoparticles were prepared and used as a core supporter for producing magnetic cross-linked enzyme aggregates (mCLEAs) from Aspergillus oryzae ST11...
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Veröffentlicht in: | Applied biochemistry and biotechnology 2020-04, Vol.190 (4), p.1319-1332 |
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description | The biodiesel production by enzymatic catalysis is the environmentally friendly production process. In this work, the polyacrylonitrile coated magnetic nanoparticles were prepared and used as a core supporter for producing magnetic cross-linked enzyme aggregates (mCLEAs) from
Aspergillus oryzae
ST11 lipase with the co-feeding of bovine serum albumin (BSA). The highest immobilized lipase activity was 0.09 U/mg-support or 81.7% of recovered activity. The resulting mCLEAs exhibited the desired characteristics; it had improved the stabilities for pH, temperature, as well as storage comparing to free enzyme. Moreover, when this biocatalyst was used for biodiesel production at the optimal conditions (30%
w/w
of mCLEAs, 30%
w/w
of water content and stepwise addition of methanol), the biodiesel conversion was 95% within 24 h of reaction, while one-step addition of methanol produced 81% conversion. The mCLEAs could be reused for 5 cycles and retained the biodiesel conversion higher than 60%. |
doi_str_mv | 10.1007/s12010-019-03196-7 |
format | Article |
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Aspergillus oryzae
ST11 lipase with the co-feeding of bovine serum albumin (BSA). The highest immobilized lipase activity was 0.09 U/mg-support or 81.7% of recovered activity. The resulting mCLEAs exhibited the desired characteristics; it had improved the stabilities for pH, temperature, as well as storage comparing to free enzyme. Moreover, when this biocatalyst was used for biodiesel production at the optimal conditions (30%
w/w
of mCLEAs, 30%
w/w
of water content and stepwise addition of methanol), the biodiesel conversion was 95% within 24 h of reaction, while one-step addition of methanol produced 81% conversion. The mCLEAs could be reused for 5 cycles and retained the biodiesel conversion higher than 60%.</description><identifier>ISSN: 0273-2289</identifier><identifier>EISSN: 1559-0291</identifier><identifier>DOI: 10.1007/s12010-019-03196-7</identifier><identifier>PMID: 31754983</identifier><language>eng</language><publisher>New York: Springer US</publisher><subject>Acrylic Resins - chemistry ; Aggregates ; Animals ; Aspergillus oryzae ; Aspergillus oryzae - enzymology ; Biocatalysis ; Biochemistry ; Biodiesel fuels ; Biofuels ; Biotechnology ; Bovine serum albumin ; Catalysis ; Cattle ; Chemistry ; Chemistry and Materials Science ; Conversion ; Crosslinking ; Diesel ; Enzymes ; Enzymes - chemistry ; Enzymes, Immobilized - chemistry ; Hydrogen-Ion Concentration ; Lipase ; Lipase - chemistry ; Magnetics ; Magnetite Nanoparticles - chemistry ; Methanol ; Moisture content ; Nanoparticles ; Polyacrylonitrile ; Serum albumin ; Serum Albumin, Bovine - chemistry ; Spectrophotometry, Infrared ; Temperature ; Water content</subject><ispartof>Applied biochemistry and biotechnology, 2020-04, Vol.190 (4), p.1319-1332</ispartof><rights>Springer Science+Business Media, LLC, part of Springer Nature 2019</rights><rights>Springer Science+Business Media, LLC, part of Springer Nature 2019.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c412t-5834f29baba8e5387d3694206febd2af3a3d44d68dab97ad8459e929c1f96f983</citedby><cites>FETCH-LOGICAL-c412t-5834f29baba8e5387d3694206febd2af3a3d44d68dab97ad8459e929c1f96f983</cites><orcidid>0000-0002-5578-9737</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s12010-019-03196-7$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s12010-019-03196-7$$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/31754983$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Paitaid, Pattarapon</creatorcontrib><creatorcontrib>H-Kittikun, Aran</creatorcontrib><title>Magnetic Cross-Linked Enzyme Aggregates of Aspergillus oryzae ST11 Lipase Using Polyacrylonitrile Coated Magnetic Nanoparticles for Biodiesel Production</title><title>Applied biochemistry and biotechnology</title><addtitle>Appl Biochem Biotechnol</addtitle><addtitle>Appl Biochem Biotechnol</addtitle><description>The biodiesel production by enzymatic catalysis is the environmentally friendly production process. In this work, the polyacrylonitrile coated magnetic nanoparticles were prepared and used as a core supporter for producing magnetic cross-linked enzyme aggregates (mCLEAs) from
Aspergillus oryzae
ST11 lipase with the co-feeding of bovine serum albumin (BSA). The highest immobilized lipase activity was 0.09 U/mg-support or 81.7% of recovered activity. The resulting mCLEAs exhibited the desired characteristics; it had improved the stabilities for pH, temperature, as well as storage comparing to free enzyme. Moreover, when this biocatalyst was used for biodiesel production at the optimal conditions (30%
w/w
of mCLEAs, 30%
w/w
of water content and stepwise addition of methanol), the biodiesel conversion was 95% within 24 h of reaction, while one-step addition of methanol produced 81% conversion. The mCLEAs could be reused for 5 cycles and retained the biodiesel conversion higher than 60%.</description><subject>Acrylic Resins - chemistry</subject><subject>Aggregates</subject><subject>Animals</subject><subject>Aspergillus oryzae</subject><subject>Aspergillus oryzae - enzymology</subject><subject>Biocatalysis</subject><subject>Biochemistry</subject><subject>Biodiesel fuels</subject><subject>Biofuels</subject><subject>Biotechnology</subject><subject>Bovine serum albumin</subject><subject>Catalysis</subject><subject>Cattle</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Conversion</subject><subject>Crosslinking</subject><subject>Diesel</subject><subject>Enzymes</subject><subject>Enzymes - chemistry</subject><subject>Enzymes, Immobilized - chemistry</subject><subject>Hydrogen-Ion Concentration</subject><subject>Lipase</subject><subject>Lipase - chemistry</subject><subject>Magnetics</subject><subject>Magnetite Nanoparticles - chemistry</subject><subject>Methanol</subject><subject>Moisture content</subject><subject>Nanoparticles</subject><subject>Polyacrylonitrile</subject><subject>Serum albumin</subject><subject>Serum Albumin, Bovine - 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chemistry</topic><topic>Aggregates</topic><topic>Animals</topic><topic>Aspergillus oryzae</topic><topic>Aspergillus oryzae - enzymology</topic><topic>Biocatalysis</topic><topic>Biochemistry</topic><topic>Biodiesel fuels</topic><topic>Biofuels</topic><topic>Biotechnology</topic><topic>Bovine serum albumin</topic><topic>Catalysis</topic><topic>Cattle</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>Conversion</topic><topic>Crosslinking</topic><topic>Diesel</topic><topic>Enzymes</topic><topic>Enzymes - chemistry</topic><topic>Enzymes, Immobilized - chemistry</topic><topic>Hydrogen-Ion Concentration</topic><topic>Lipase</topic><topic>Lipase - chemistry</topic><topic>Magnetics</topic><topic>Magnetite Nanoparticles - chemistry</topic><topic>Methanol</topic><topic>Moisture content</topic><topic>Nanoparticles</topic><topic>Polyacrylonitrile</topic><topic>Serum albumin</topic><topic>Serum Albumin, Bovine - chemistry</topic><topic>Spectrophotometry, Infrared</topic><topic>Temperature</topic><topic>Water content</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Paitaid, Pattarapon</creatorcontrib><creatorcontrib>H-Kittikun, Aran</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>Environment Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</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>Environmental Sciences and Pollution Management</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 Basic</collection><collection>Genetics Abstracts</collection><collection>Environment Abstracts</collection><jtitle>Applied biochemistry and biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Paitaid, Pattarapon</au><au>H-Kittikun, Aran</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Magnetic Cross-Linked Enzyme Aggregates of Aspergillus oryzae ST11 Lipase Using Polyacrylonitrile Coated Magnetic Nanoparticles for Biodiesel Production</atitle><jtitle>Applied biochemistry and biotechnology</jtitle><stitle>Appl Biochem Biotechnol</stitle><addtitle>Appl Biochem Biotechnol</addtitle><date>2020-04-01</date><risdate>2020</risdate><volume>190</volume><issue>4</issue><spage>1319</spage><epage>1332</epage><pages>1319-1332</pages><issn>0273-2289</issn><eissn>1559-0291</eissn><abstract>The biodiesel production by enzymatic catalysis is the environmentally friendly production process. In this work, the polyacrylonitrile coated magnetic nanoparticles were prepared and used as a core supporter for producing magnetic cross-linked enzyme aggregates (mCLEAs) from
Aspergillus oryzae
ST11 lipase with the co-feeding of bovine serum albumin (BSA). The highest immobilized lipase activity was 0.09 U/mg-support or 81.7% of recovered activity. The resulting mCLEAs exhibited the desired characteristics; it had improved the stabilities for pH, temperature, as well as storage comparing to free enzyme. Moreover, when this biocatalyst was used for biodiesel production at the optimal conditions (30%
w/w
of mCLEAs, 30%
w/w
of water content and stepwise addition of methanol), the biodiesel conversion was 95% within 24 h of reaction, while one-step addition of methanol produced 81% conversion. The mCLEAs could be reused for 5 cycles and retained the biodiesel conversion higher than 60%.</abstract><cop>New York</cop><pub>Springer US</pub><pmid>31754983</pmid><doi>10.1007/s12010-019-03196-7</doi><tpages>14</tpages><orcidid>https://orcid.org/0000-0002-5578-9737</orcidid></addata></record> |
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subjects | Acrylic Resins - chemistry Aggregates Animals Aspergillus oryzae Aspergillus oryzae - enzymology Biocatalysis Biochemistry Biodiesel fuels Biofuels Biotechnology Bovine serum albumin Catalysis Cattle Chemistry Chemistry and Materials Science Conversion Crosslinking Diesel Enzymes Enzymes - chemistry Enzymes, Immobilized - chemistry Hydrogen-Ion Concentration Lipase Lipase - chemistry Magnetics Magnetite Nanoparticles - chemistry Methanol Moisture content Nanoparticles Polyacrylonitrile Serum albumin Serum Albumin, Bovine - chemistry Spectrophotometry, Infrared Temperature Water content |
title | Magnetic Cross-Linked Enzyme Aggregates of Aspergillus oryzae ST11 Lipase Using Polyacrylonitrile Coated Magnetic Nanoparticles for Biodiesel Production |
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