Immobilization of Candida cylindracea Lipase by Covalent Attachment on Glu-Modified Bentonite
Alkaline Ca-bentonite, obtained upon acid activation and base load of natural bentonite, has a good anion exchange capability. Glu-modified alkaline Ca-bentonites were further prepared by covalent binding with glutamic acid for the immobilization of lipase OF from Candida cylindracea . The obtained...
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| creator | Tang, Aixing Zhang, Yiqin Wei, Tengyou Wu, Jian Li, Qingyun Liu, Youyan |
| description | Alkaline Ca-bentonite, obtained upon acid activation and base load of natural bentonite, has a good anion exchange capability. Glu-modified alkaline Ca-bentonites were further prepared by covalent binding with glutamic acid for the immobilization of lipase OF from
Candida cylindracea
. The obtained immobilized lipase demonstrated a significantly higher catalytic activity than that of unmodified alkaline Ca-bentonite, giving a specific activity of 62.1 U mg
−1
protein, twice that of the unmodified carrier, and a total activity of 391.2 U g
−1
support, retaining ~ 82.3% of the activity after being reused five times for olive oil emulsion hydrolysis. X-ray diffraction and Fourier transform infrared spectroscopy assays demonstrated the successful immobilization of the lipase on the surface of the bentonite. Upon immobilization, the thermostability of the lipase improved remarkably. At 50 °C, free lipase retained only 6.0% of its initial activity at 6 h, in comparison with 15% for Ca-Bent-lipase and 50% for Glu-Ca-Bent-lipase after 8 h. The Glu-Ca-Bent-lipase is proved as an effective biocatalyst for the biodiesel preparation, improving the transesterification reaction conversion from 52.8% in the condition of free lipase to 99.9% and keeping at 56.2% after being reused five times, while the free lipase was inactive upon two reuses. The above results provide a new route in the use of inexpensive bentonite for the enzyme immobilization. |
| doi_str_mv | 10.1007/s12010-018-2838-8 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_osti_</sourceid><recordid>TN_cdi_osti_scitechconnect_22927820</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2084663822</sourcerecordid><originalsourceid>FETCH-LOGICAL-c437t-4f2abdf21d47b82723ab76ab98bf3e50956b66f8fc652baf79635385cda81c013</originalsourceid><addsrcrecordid>eNp1kUFvFCEYhonR2G31B3gxk3jxgsLHMDDHutG2yRov7dEQYMDSzMA6ME22v142U6uXniDwvO-XLw9C7yj5RAkRnzMFQgkmVGKQTGL5Am0o5z0m0NOXaENAMAwg-xN0mvMdIRQkF6_RCSNESmjpBv28mqZkwhgedAkpNsk3Wx2HMOjGHsYQh1lbp5td2OvsGnNotulejy6W5rwUbW-n47XmLsYFf09D8MENzZf6mGIo7g165fWY3dvH8wzdfPt6vb3Eux8XV9vzHbYtEwW3HrQZPNChFUaCAKaN6LTppfHMcdLzznSdl952HIz2ou8YZ5LbQUtqCWVn6MPam3IJKts62t7aFKOzRQH0ICSQSn1cqf2cfi8uFzWFbN046ujSkhUQybuOUfpf4RN6l5Y51h2OVFspCVApulJ2TjnPzqv9HCY9HxQl6mhIrYZUNaSOhpSsmfePzYuZ3PCU-KukArACuX7FX27-N_r51j85vpoh</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2084663822</pqid></control><display><type>article</type><title>Immobilization of Candida cylindracea Lipase by Covalent Attachment on Glu-Modified Bentonite</title><source>SpringerNature Journals</source><creator>Tang, Aixing ; Zhang, Yiqin ; Wei, Tengyou ; Wu, Jian ; Li, Qingyun ; Liu, Youyan</creator><creatorcontrib>Tang, Aixing ; Zhang, Yiqin ; Wei, Tengyou ; Wu, Jian ; Li, Qingyun ; Liu, Youyan</creatorcontrib><description>Alkaline Ca-bentonite, obtained upon acid activation and base load of natural bentonite, has a good anion exchange capability. Glu-modified alkaline Ca-bentonites were further prepared by covalent binding with glutamic acid for the immobilization of lipase OF from
Candida cylindracea
. The obtained immobilized lipase demonstrated a significantly higher catalytic activity than that of unmodified alkaline Ca-bentonite, giving a specific activity of 62.1 U mg
−1
protein, twice that of the unmodified carrier, and a total activity of 391.2 U g
−1
support, retaining ~ 82.3% of the activity after being reused five times for olive oil emulsion hydrolysis. X-ray diffraction and Fourier transform infrared spectroscopy assays demonstrated the successful immobilization of the lipase on the surface of the bentonite. Upon immobilization, the thermostability of the lipase improved remarkably. At 50 °C, free lipase retained only 6.0% of its initial activity at 6 h, in comparison with 15% for Ca-Bent-lipase and 50% for Glu-Ca-Bent-lipase after 8 h. The Glu-Ca-Bent-lipase is proved as an effective biocatalyst for the biodiesel preparation, improving the transesterification reaction conversion from 52.8% in the condition of free lipase to 99.9% and keeping at 56.2% after being reused five times, while the free lipase was inactive upon two reuses. The above results provide a new route in the use of inexpensive bentonite for the enzyme immobilization.</description><identifier>ISSN: 0273-2289</identifier><identifier>EISSN: 1559-0291</identifier><identifier>DOI: 10.1007/s12010-018-2838-8</identifier><identifier>PMID: 30088241</identifier><language>eng</language><publisher>New York: Springer US</publisher><subject>60 APPLIED LIFE SCIENCES ; Anion exchange ; Anion exchanging ; BENTONITE ; Biochemistry ; BIODIESEL FUELS ; Biofuels ; Biotechnology ; Calcium ; CANDIDA ; Candida cylindracea ; Catalysis ; Catalytic activity ; CHEMICAL BONDS ; Chemistry ; Chemistry and Materials Science ; FOURIER TRANSFORM SPECTROMETERS ; Fourier transforms ; GLUTAMIC ACID ; HYDROLYSIS ; Immobilization ; Infrared spectroscopy ; ION EXCHANGE ; Lipase ; LIPASES ; Oils & fats ; OLIVE OIL ; Proteins ; Thermal stability ; Transesterification ; X-RAY DIFFRACTION</subject><ispartof>Applied biochemistry and biotechnology, 2019-03, Vol.187 (3), p.870-883</ispartof><rights>Springer Science+Business Media, LLC, part of Springer Nature 2018</rights><rights>Applied Biochemistry and Biotechnology is a copyright of Springer, (2018). All Rights Reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c437t-4f2abdf21d47b82723ab76ab98bf3e50956b66f8fc652baf79635385cda81c013</citedby><cites>FETCH-LOGICAL-c437t-4f2abdf21d47b82723ab76ab98bf3e50956b66f8fc652baf79635385cda81c013</cites><orcidid>0000-0003-4459-7841</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/s12010-018-2838-8$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s12010-018-2838-8$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>230,314,780,784,885,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/30088241$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/22927820$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Tang, Aixing</creatorcontrib><creatorcontrib>Zhang, Yiqin</creatorcontrib><creatorcontrib>Wei, Tengyou</creatorcontrib><creatorcontrib>Wu, Jian</creatorcontrib><creatorcontrib>Li, Qingyun</creatorcontrib><creatorcontrib>Liu, Youyan</creatorcontrib><title>Immobilization of Candida cylindracea Lipase by Covalent Attachment on Glu-Modified Bentonite</title><title>Applied biochemistry and biotechnology</title><addtitle>Appl Biochem Biotechnol</addtitle><addtitle>Appl Biochem Biotechnol</addtitle><description>Alkaline Ca-bentonite, obtained upon acid activation and base load of natural bentonite, has a good anion exchange capability. Glu-modified alkaline Ca-bentonites were further prepared by covalent binding with glutamic acid for the immobilization of lipase OF from
Candida cylindracea
. The obtained immobilized lipase demonstrated a significantly higher catalytic activity than that of unmodified alkaline Ca-bentonite, giving a specific activity of 62.1 U mg
−1
protein, twice that of the unmodified carrier, and a total activity of 391.2 U g
−1
support, retaining ~ 82.3% of the activity after being reused five times for olive oil emulsion hydrolysis. X-ray diffraction and Fourier transform infrared spectroscopy assays demonstrated the successful immobilization of the lipase on the surface of the bentonite. Upon immobilization, the thermostability of the lipase improved remarkably. At 50 °C, free lipase retained only 6.0% of its initial activity at 6 h, in comparison with 15% for Ca-Bent-lipase and 50% for Glu-Ca-Bent-lipase after 8 h. The Glu-Ca-Bent-lipase is proved as an effective biocatalyst for the biodiesel preparation, improving the transesterification reaction conversion from 52.8% in the condition of free lipase to 99.9% and keeping at 56.2% after being reused five times, while the free lipase was inactive upon two reuses. The above results provide a new route in the use of inexpensive bentonite for the enzyme immobilization.</description><subject>60 APPLIED LIFE SCIENCES</subject><subject>Anion exchange</subject><subject>Anion exchanging</subject><subject>BENTONITE</subject><subject>Biochemistry</subject><subject>BIODIESEL FUELS</subject><subject>Biofuels</subject><subject>Biotechnology</subject><subject>Calcium</subject><subject>CANDIDA</subject><subject>Candida cylindracea</subject><subject>Catalysis</subject><subject>Catalytic activity</subject><subject>CHEMICAL BONDS</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>FOURIER TRANSFORM SPECTROMETERS</subject><subject>Fourier transforms</subject><subject>GLUTAMIC ACID</subject><subject>HYDROLYSIS</subject><subject>Immobilization</subject><subject>Infrared spectroscopy</subject><subject>ION EXCHANGE</subject><subject>Lipase</subject><subject>LIPASES</subject><subject>Oils & fats</subject><subject>OLIVE OIL</subject><subject>Proteins</subject><subject>Thermal stability</subject><subject>Transesterification</subject><subject>X-RAY 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transforms</topic><topic>GLUTAMIC ACID</topic><topic>HYDROLYSIS</topic><topic>Immobilization</topic><topic>Infrared spectroscopy</topic><topic>ION EXCHANGE</topic><topic>Lipase</topic><topic>LIPASES</topic><topic>Oils & fats</topic><topic>OLIVE OIL</topic><topic>Proteins</topic><topic>Thermal stability</topic><topic>Transesterification</topic><topic>X-RAY DIFFRACTION</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tang, Aixing</creatorcontrib><creatorcontrib>Zhang, Yiqin</creatorcontrib><creatorcontrib>Wei, Tengyou</creatorcontrib><creatorcontrib>Wu, Jian</creatorcontrib><creatorcontrib>Li, Qingyun</creatorcontrib><creatorcontrib>Liu, Youyan</creatorcontrib><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 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Biotechnol</addtitle><date>2019-03-01</date><risdate>2019</risdate><volume>187</volume><issue>3</issue><spage>870</spage><epage>883</epage><pages>870-883</pages><issn>0273-2289</issn><eissn>1559-0291</eissn><abstract>Alkaline Ca-bentonite, obtained upon acid activation and base load of natural bentonite, has a good anion exchange capability. Glu-modified alkaline Ca-bentonites were further prepared by covalent binding with glutamic acid for the immobilization of lipase OF from
Candida cylindracea
. The obtained immobilized lipase demonstrated a significantly higher catalytic activity than that of unmodified alkaline Ca-bentonite, giving a specific activity of 62.1 U mg
−1
protein, twice that of the unmodified carrier, and a total activity of 391.2 U g
−1
support, retaining ~ 82.3% of the activity after being reused five times for olive oil emulsion hydrolysis. X-ray diffraction and Fourier transform infrared spectroscopy assays demonstrated the successful immobilization of the lipase on the surface of the bentonite. Upon immobilization, the thermostability of the lipase improved remarkably. At 50 °C, free lipase retained only 6.0% of its initial activity at 6 h, in comparison with 15% for Ca-Bent-lipase and 50% for Glu-Ca-Bent-lipase after 8 h. The Glu-Ca-Bent-lipase is proved as an effective biocatalyst for the biodiesel preparation, improving the transesterification reaction conversion from 52.8% in the condition of free lipase to 99.9% and keeping at 56.2% after being reused five times, while the free lipase was inactive upon two reuses. The above results provide a new route in the use of inexpensive bentonite for the enzyme immobilization.</abstract><cop>New York</cop><pub>Springer US</pub><pmid>30088241</pmid><doi>10.1007/s12010-018-2838-8</doi><tpages>14</tpages><orcidid>https://orcid.org/0000-0003-4459-7841</orcidid></addata></record> |
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| ispartof | Applied biochemistry and biotechnology, 2019-03, Vol.187 (3), p.870-883 |
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| source | SpringerNature Journals |
| subjects | 60 APPLIED LIFE SCIENCES Anion exchange Anion exchanging BENTONITE Biochemistry BIODIESEL FUELS Biofuels Biotechnology Calcium CANDIDA Candida cylindracea Catalysis Catalytic activity CHEMICAL BONDS Chemistry Chemistry and Materials Science FOURIER TRANSFORM SPECTROMETERS Fourier transforms GLUTAMIC ACID HYDROLYSIS Immobilization Infrared spectroscopy ION EXCHANGE Lipase LIPASES Oils & fats OLIVE OIL Proteins Thermal stability Transesterification X-RAY DIFFRACTION |
| title | Immobilization of Candida cylindracea Lipase by Covalent Attachment on Glu-Modified Bentonite |
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